Lipopeptide Peptide

Lipopeptide, characterized by the sequence Palmitoyl-Gly-Gln-Pro-Arg, is a palmitoylated fragment derived from immunoglobulin G (IgG). IgG is a type of antibody, considered a crucial component of the immune system that apparently mediates various inflammatory processes. The palmitoylation of this peptide fragment, which involves the attachment of a palmitic acid molecule, may also enhance its experimental potential. This modification appears to improve the lipopeptide’s ability to penetrate through the corneal layers of skin tissue models. The increased penetration appears to be due to the added lipid (fat) component, which aids in traversing the lipid-rich environment of the outer layers of skin tissue.

Chemical Makeup

Molecular formula: C₃₈H₆₈N₆O₈
Molecular weight: 736.9 g/mol
Sequence: Pal-Gly-Gln-Pro-Arg
Other known titles: Pal-GQPR, Palmitoyl Tetrapeptide-7/3

Research and Clinical Studies

The summary below reflects the latest findings from preliminary studies on the functionalities of Lipopeptide, as revealed through diverse experimental methods.

Lipopeptide and the Extracellular Dermal Matrix

One study conducted a series of evaluations on a blend of peptides including Lipopeptide (Pal-GQPR) for their potential action on skin cell structure.⁽¹⁾ Echography tests suggested that this blend might reduce the thickness of the subepidermal low-echogenic band and support its density, indicating a possible improvement in skin structure. Moreover, studies in murine models hinted that these peptides might potentially enhance the extracellular dermal matrix structure compared to a placebo. More specifically it was posited that this compound might also play a role in decreasing the secretion of interleukin-6 (IL-6), a cytokine involved in inflammatory responses. IL-6 is a molecule that is typically associated with immune responses and appears to be elevated during inflammation, potentially contributing to various inflammatory skin conditions. The possible reduction of IL-6 secretion by Lipopeptide suggests that it may aid in mitigating inflammation, especially following UVB radiation exposure, a common cause of skin cell inflammation and damage. Additionally, Lipopeptide is thought to potentially stimulate the production of critical structural components around skin cells, such as laminin IV and V, as well as collagen VII. Laminins, particularly types IV and V, are integral components of the basement membrane, a layer that supports epithelial cells and is considered essential for tissue integrity. They play a crucial role in cell adhesion, differentiation, and migration, which are vital for skin repair and maintenance. Collagen VII, on the other hand, is a key component of anchoring fibrils that provide structural support and stability to the skin. It is essential for the attachment of the epidermis to the underlying dermis. The stimulation of these components by Lipopeptide may imply a potential role in enhancing the skin’s structural framework.⁽²⁾ Other researchers have also commented that Lipopeptide may have an action “as an anti-inflammatory agent and has anti-aging and skin firming [potential].”⁽³⁾

Lipopeptide and Photoaged Skin Cells

The potential of Lipopeptide was investigated in a randomized controlled trial (RCT) as a blend alongside other peptides and active ingredients. This peptide, along with other compounds, such as retinyl palmitate and natural extracts, was assessed for its potential in improving the appearance of photoaged skin cells. Twelve days into the experiment, the peptide was observed to have stimulated the deposition of fibrillin-1 in the skin, a marker for skin repair, compared to the baseline levels. This was comparable to the apparent results observed with all-trans retinoic acid (RA), considered to be a clinical standard for photoaged skin cells. The accumulation of fibrillin-1 indicates a potential structural change in the skin, although this alone does not confirm the success of the experiment. In a 6-month RCT the peptide appeared to potentiate an improvement in skin wrinkles compared to the baseline. Interestingly, this potential improvement became more pronounced after 12 months. The vehicle formulation, which lacked the active ingredients, did not show similar results, suggesting that the ingredients in the test product, including Lipopeptide, may contribute to the observed effects. Furthermore, the study investigated the distribution of fibrillin-1 in skin biopsies from the RCT. Skin applied with the Lipopeptide appeared to have a significant increase in fibrillin-1 in the papillary dermis compared to the placebo group. This supports the idea that long-term experiments with Lipopeptide may lead to a visible improvement in the photoaged skin. The researchers concluded that Lipopeptide may “produce significant improvement in the appearance of wrinkles and further supports the [study] of fibrillin-1 as a robust biomarker for the repair of photoaged dermis.”⁽⁴⁾

Lipopeptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.

References:

1. Mondon, P., Hillion, M., Peschard, O., Andre, N., Marchand, T., Doridot, E., Feuilloley, M. G., Pionneau, C., & Chardonnet, S. (2015). Evaluation of dermal extracellular matrix and epidermal-dermal junction modifications using matrix-assisted laser desorption/ionization mass spectrometric imaging, in vivo reflectance confocal microscopy, echography, and histology: effect of age and peptide applications. Journal of cosmetic dermatology, 14(2), 152–160. https://doi.org/10.1111/jocd.12135
2. Resende, D. I. S. P., Ferreira, M. S., Sousa-Lobo, J. M., Sousa, E., & Almeida, I. F. (2021). Usage of Synthetic Peptides in Cosmetics for Sensitive Skin. Pharmaceuticals (Basel, Switzerland), 14(8), 702. https://doi.org/10.3390/ph14080702
3. Fadilah, N. I. M., Rahman, M. B. A., Yusof, L. M., Mustapha, N. M., & Ahmad, H. (2021). The Therapeutic Effect and In Vivo Assessment of Palmitoyl-GDPH on the Wound Healing Process. Pharmaceutics, 13(2), 193. https://doi.org/10.3390/pharmaceutics13020193
4. Watson, R. E., Ogden, S., Cotterell, L. F., Bowden, J. J., Bastrilles, J. Y., Long, S. P., & Griffiths, C. E. (2009). Effects of a cosmetic ‘anti-ageing’ product improves photoaged skin [corrected]. The British journal of dermatology, 161(2), 419–426. https://doi.org/10.1111/j.1365-2133.2009.09216.x

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Pal-GHK Peptide

Palmitoyl-GHK, also known as palmitoyl-tripeptide-1, is a synthetic hybrid molecule consisting of a chain of three amino acids attached to a palmitic acid molecule. The GHK sequence, which consists of the amino acids Gly-His-Lys, is found naturally in plasma, discovered in 1973 by Pickart et al.⁽¹⁾ The addition of palmitoyl to the molecule is thought to result in better penetration through the stratum corneum of the epidermal barrier.⁽²⁾ The palmitoyl group, which is a fatty acid chain, is thought to increase lipophilicity, which may potentially enhance the compatibility of the molecule with the lipid-rich environment of the stratum corneum. The added palmitoyl group might also act as a penetration enhancer by disrupting the tightly packed lipid structure of the stratum corneum. This disruption could temporarily loosen the lipid matrix, allowing Pal-GHK and other agents to permeate through various skin tissue models.

Researchers have suggested that Pal-GHK may stimulate collagen production, a key component of the skin’s extracellular matrix (ECM). This hypothesis was initially developed because the Gly-His-Lys sequence is also a structural fragment of the protein collagen. Gly-His-Lys is believed to be released during collagen hydrolysis, typically induced in tissue repair and to mitigate inflammation. Therefore, the tripeptide is believed to act as a natural feedback signal to fibroblasts, the cells responsible for producing collagen and other ECM components.

Pal-GHK may also exhibit antioxidant potential against damage caused by free radicals. Free radicals are unstable molecules that may damage cell structures and are considered to contribute to the aging process. By potentially neutralizing free radicals, Palmitoyl-GHK may reduce cellular aging and inflammation.

Chemical Makeup

Molecular formula: C₃₀H₅₄N₆O₅
Molecular weight: 578.8 g/mol
Other Known Titles: Palmitoyl Tripeptide-1, Palmitoyl oligopeptide, Biopeptide-CL

Research and Clinical Studies

Pal-GHK and Collagen Synthesis

Research by Maquart et al. dating back to 1988 and published in the journal FEBS Letters suggests that the Gly-His-Lys in Pal-GHK is a fragment produced during the hydrolysis of collagen.⁽³⁾ Such fragments are produced when collagen is damaged, and they may signal fibroblasts to initiate the process of collagen synthesis. Pal-GHK may have a similar potential to stimulate collagen, elastin, and glycosaminoglycans, important components of the extracellular matrix of the skin. The researchers concluded, “The presence of a GHK triplet in the alpha 2(I) chain of type I collagen suggests that the tripeptide might be liberated by proteases at the site of a wound and exert in situ healing effects.”

A placebo-controlled clinical study suggests that Pal-GHK may stimulate collagen synthesis, as concluded following the assessment of the apparent effect of the peptide on skin thickness. The trial involved twenty-three subjects, and the researchers reported a small but statistically significant increase in skin thickness of about 4% compared to the placebo.⁽⁵⁾

Pal-GHK and Wrinkle Depth

A clinical study was conducted to ascertain the peptide’s potential in reducing the depth and length of wrinkles along the stratum corneum. The study evaluated the action of the peptide in a cream form ⁽⁶⁾ and included fifteen subjects. The scientists reported an apparent reduction in wrinkle length, depth, and texture inconsistency (roughness) following the study period.

Another clinical experiment involved a combination of Pal-GHK tripeptide and another palmitoylated peptide called Pal-GQPR.⁽⁷⁾ Pal-GQPR is a tetrapeptide with the sequence of Pal-Gly-Gln-Pro-Arg, and it is a fragment of immunoglobulin G (IgG) which is considered to play an important role in reducing the amount of interleukin 6 (IL6) production. The design was a blind, randomized clinical study that included twenty-eight subjects. There was an apparent reduction of wrinkle depth, volume, density, texture inconsistency, and the area occupied by deep wrinkles following exposure to the combination of the two palmitoylated peptides.

Pal-GHK and Antioxidation

A 2018 laboratory experiment by Sakuma et al. suggested that the amino-acid sequence of Pal-GHK may have antioxidative potential.⁽⁸⁾ The researchers also reported that this potential was apparently more powerful than other compounds classified as antioxidative and commonly used in research, such as carnosine and reduced glutathione. More specifically, the researchers shared that “Experiments utilizing an ESR spin-trapping technique revealed that, among hydroxyl (·OH), superoxide (O2-·), and peroxyl (ROO·) radicals generated by respective chemical reaction systems, GHK diminished signals of both ·OH and ROO·.”

Active radicals appear to be apparent mediators of photodamage. Examples of such active radicals include reactive oxygen species (ROS), reactive nitrogen species (RNS), and reactive carbonyl species (RCS), which are considered to cause harm to lipids, DNA, and proteins. Studies have suggested that the amino acid sequence found in Pal-GHK may potentially prevent protein glycation and may possess anti-RCS properties against various radicals like acrolein, malondialdehyde, and 4-hydroxynoneal.⁽⁹⁾

Additionally, Pal-GHK has been suggested to have the potential to reduce the release of iron from ferritin, which catalyzes lipid peroxidation. In other words, Pal-GHK may lead to a lower rate of lipid peroxidation, ostensibly preserving the integrity of cell membranes and reducing cellular damage. In the context of skin tissue integrity, this might contribute to enhanced skin cell function and survival. One study shared results of an apparent 87% decrease in the iron release from damaged tissue using Pal-GHK, which appeared to have reduced oxidation in the affected tissues.⁽¹⁰⁾ By potentially lowering lipid peroxidation, Pal-GHK might indirectly help mitigate the alteration of DNA and proteins, potentially reducing risk factors that may otherwise lead to cellular damage.

Pal-GHK may also potentially reduce the production of reactive oxygen species and inflammatory cytokines while increasing the activity of antioxidant enzymes. During one experiment using a murine model, Pal-GHK was suggested to suppress the activation of Nuclear Factor kappa-light-chain-enhancer of activated B cells (NF-κB) and p38 mitogen-activated protein kinase (MAPK) signaling pathways, both of which are associated with inflammation.⁽¹¹⁾ Pal-GHK might potentially inhibit the activation of p38 MAPK either by blocking the upstream kinases that activate it or by interfering with the signaling molecules that initiate its phosphorylation. The inhibition may conceivably suppress the inflammatory response, reducing the overall stress on cells. This may lead to reduced infiltration of inflammatory cells in the tissues of murine models of lung tissue damage and lower levels of TNF-1 and IL-6 production.

Researchers have also speculated about Pal-GHK’s potential to alleviate the oxidative stress of smoke inhalation. Research findings have led to the proposal that the amino-acid sequence of Pal-GHK might impede oxidative stress in alveolar epithelial cells by increasing Nrf2 (Nuclear factor erythroid 2-related factor 2) expression and reducing the levels of reactive oxygen species in cell cultures.⁽¹²⁾ Nrf2 is a protein that may regulate the expression of antioxidant proteins that protect against oxidative damage triggered by injury and inflammation.

Pal-GHK peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.

References:

1. Pickart, L., & Thaler, M. M. (1973). Tripeptide in human serum which prolongs survival of normal liver cells and stimulates growth in neoplastic liver. Nature: New biology, 243(124), 85–87.
2. Gorouhi, F., & Maibach, H. I. (2009). Role of peptides in preventing or treating aged skin. International journal of cosmetic science, 31(5), 327-345.
3. Maquart, F. X., Pickart, L., Laurent, M., Gillery, P., Monboisse, J. C., & Borel, J. P. (1988). Stimulation of collagen synthesis in fibroblast cultures by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+. FEBS letters, 238(2), 343–346. https://doi.org/10.1016/0014-5793(88)80509-x
4. Trookman, N. S., Rizer, R. L., Ford, R., Mehta, R., & Gotz, V. (2009). Clinical assessment of a combination lip treatment to restore moisturization and fullness. The Journal of clinical and aesthetic dermatology, 2(12), 44–48.
5. Lintner, K., & Peschard, O. (2000). Biologically active peptides: from a laboratory bench curiosity to a functional skin care product. International journal of cosmetic science, 22(3), 207–218. https://doi.org/10.1046/j.1467-2494.2000.00010.x
6. Schagen, S. K. (2017). Peptide treatments with effective anti-aging results. Cosmetics, 4(2), 16.
7. Fournial, A., & Mondon, P. New Cosmetic or Dermopharmaceutical Use of a Mixture of a Ghk Tripeptide and Gqpr Tetrapeptide.
8. Sakuma, S., Ishimura, M., Yuba, Y., Itoh, Y., & Fujimoto, Y. (2018). The peptide glycyl-ʟ-histidyl-ʟ-lysine is an endogenous antioxidant in living organisms, possibly by diminishing hydroxyl and peroxyl radicals. International journal of physiology, pathophysiology and pharmacology, 10(3), 132–138.
9. Cebrián, J., Messeguer, A., Facino, R. M., & García Antón, J. M. (2005). New anti-RNS and -RCS products for cosmetic treatment. International journal of cosmetic science, 27(5), 271–278. https://doi.org/10.1111/j.1467-2494.2005.00279.x
10. Park, J. R., Lee, H., Kim, S. I., & Yang, S. R. (2016). The tri-peptide GHK-Cu complex ameliorates lipopolysaccharide-induced acute lung injury in mice. Oncotarget, 7(36), 58405–58417. https://doi.org/10.18632/oncotarget.11168
11. Sakuma, S., Ishimura, M., Yuba, Y., Itoh, Y., & Fujimoto, Y. (2018). The peptide glycyl-ʟ-histidyl-ʟ-lysine is an endogenous antioxidant in living organisms, possibly by diminishing hydroxyl and peroxyl radicals. International journal of physiology, pathophysiology and pharmacology, 10(3), 132–138.
12. Zhang, Q., Yan, L., Lu, J., & Zhou, X. (2022). Glycyl-L-histidyl-L-lysine-Cu2+ attenuates cigarette smoke-induced pulmonary emphysema and inflammation by reducing oxidative stress pathway. Frontiers in molecular biosciences, 9, 925700. https://doi.org/10.3389/fmolb.2022.925700

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Palmitoyl Tetrapeptide-7

Palmitoyl Tetrapeptide-7 is a small peptide composed of four amino acids: palmitoyl, glycine, glutamine, and arginine.⁽¹⁾ It is a synthetic peptide analog of the natural matrikine peptide, which is considered to play a vital role in regulating extracellular matrix (ECM) turnover and other related cellular activities.

Initial research suggests that the Palmitoyl Tetrapeptide-7 peptide may stimulate the synthesis of ECM components, such as collagen and elastin, and may inhibit the production of pro-inflammatory cytokines. It has also been hypothesized to modulate gene expression involved in ECM remodeling, cell proliferation, and inflammation.⁽²⁾

Moreover, Palmitoyl Tetrapeptide-7 may function by suppressing the activity of interleukin-6 (IL-6), a pro-inflammatory cytokine that plays a role in the apoptosis of skin cells (cell aging and death) and inflammation. IL-6 secretion is considered to increase with time, leading to the degradation of the ECM, and resulting in a loss of flexibility and structural integrity in the skin barrier.

Chemical Makeup⁽¹⁾

Molecular Formula: C₃₄H₆₂N₈O₇
Molecular Weight: 694.9 g/mol
Other Known Titles: Pal-Gly-Gln-Pro-Arg-OH, N-Palmitoylrigin , Palmitoyl-GQPR, Rigin

Research and Clinical Studies

Palmitoyl Tetrapeptide-7 Mechanism of Action

Based on animal studies, Palmitoyl Tetrapeptide-7 has been suggested to potentially inhibit the activity of matrix metalloproteinases (MMPs) in animal models.⁽³⁾ MMPs are a group of enzymes that may degrade ECM proteins during normal tissue growth. By downregulating MMP activity, Palmitoyl Tetrapeptide-7 may prevent ECM damage and may allow cells to restore and maintain the ECM. More specifically, the peptide might stimulate the production of key components of the skin’s extracellular matrix, such as laminin IV and V as well as collagen VII. Laminins may be essential for the structural stability and integrity of the basement membrane, while collagen VII is considered critical in anchoring fibrils that connect the dermis to the epidermis. By potentially enhancing the production of these molecules, Palmitoyl Tetrapeptide-7 might contribute to the maintenance and repair of the skin barrier, thereby improving skin tissue resilience. The peptide is also thought to potentially decrease IL-6 secretion, a cytokine that is believed to play a pivotal role in promoting inflammation. By possibly reducing the levels of IL-6, Palmitoyl Tetrapeptide-7 may act to diminish inflammation, particularly following UVB exposure, which is considered to trigger inflammatory responses in the skin.⁽⁴⁾

Palmitoyl Tetrapeptide-7 and Oral Conditions

Given the inhibitory potential of the peptide on matrix metalloproteinases (MMPs), research teams have thought to examine the potential action of Palmitoyl Tetrapeptide-7 in mitigating the symptoms of certain oral conditions. MMPs enzymes may break down extracellular matrix (ECM) proteins, including those in the oral cavity. While these enzymes are considered to play a role in various physiological and pathological processes, including tissue repair, wound healing, and inflammation, excessive MMP activity might result in tissue damage and may cause various oral diseases, such as periodontitis, caries, and oral cancer. Studies have also suggested that MMP activity may be upregulated in some oral conditions, including periodontitis, characterized by the destruction of periodontal tissues. The possible inhibition of MMP activity by Palmitoyl Tetrapeptide-7 might potentially prevent or slow the progression of periodontitis (and other oral ailments) by preserving the integrity of the ECM.⁽³⁾

Palmitoyl Tetrapeptide-7 and Skin Damage

Studies suggest that the peptide may stimulate the synthesis of collagen, a key component of the extracellular matrix in the skin, and may produce anti-inflammatory action, which might reduce damage caused by environmental factors such as UV radiation and pollution.

Research has suggested that combining Palmitoyl Tetrapeptide-7 with Palmitoyl Oligopeptide (Matrixyl 3000) may synergistically stimulate collagen production and reduce inflammation. This synergy, which the study describes as “dramatic,” may help improve skin texture and reduce the depth and length of wrinkling that may occur along the stratum corneum of the epidermal barrier.⁽⁵⁾

According to the studies, “Matrixyl 3000 is a synergistic combination of two skin-active peptides, Palmitoyl oligopeptide and Palmitoyl-tetrapeptide-7, which appears promising based on the preliminary data from the manufacturer… However, it remains to be proven effective by independent published clinical studies.”

As discussed, Palmitoyl Tetrapeptide-7 may be particularly targeting stimulation of collagen type VII.⁽⁴⁾ Collagen type VII is posited to be a vital component of the skin tissues’ architecture, primarily contributing to the stability and structural integrity of the dermal-epidermal junction. It is thought to play a key role in anchoring fibrils that connect the outer epidermis to the deeper dermis. This specific collagen might form a crucial part of the basement membrane, potentially serving as a scaffold that maintains the structural cohesion between these skin layers. The presence and functionality of collagen type VII are considered essential for the prevention of blistering disorders, which occur when there is a breakdown in this connection between the dermis and epidermis. Moreover, collagen type VII may also play a role in skin tissue healing. This type of collagen could be critical in skin recovery and repair by possibly facilitating the reattachment of the epidermis to the underlying tissue after an injury. It is posited that enhancing the synthesis of collagen VII might improve wound healing outcomes, particularly in environments compromised by age or dermal afflictions.

Palmitoyl Tetrapeptide-7 and Wrinkle Depth

The peptide, sometimes classified as an “anti-aging” compound, is so named due to its perceived potential action and enhancement of integral protein production within the skin, as discussed above. In a randomized, double-blind, placebo-controlled clinical study, 20 research models were presented with a cream containing Palmitoyl Tetrapeptide-7 for 12 weeks. The cream was applied twice daily to observable wrinkles along the skin.

At the end of the study period, the researchers reported that the cream containing Palmitoyl Tetrapeptide-7 appeared to have reduced the depth and length of the wrinkles compared to the placebo cream.⁽⁶⁾ The researchers also observed an apparently significant increase in skin elasticity in the group that received the Palmitoyl Tetrapeptide-7 cream.

In another study, 20 research models were exposed to the peptide compound twice a day for four weeks, and instrumental measurements were taken to assess the improvement of biomarkers of cell aging and ECM decline. The study reported an apparent reduction in fine wrinkles by 5.97% after two weeks and 14.07% after four weeks, and a reported increase in skin elasticity by 6.81% after two weeks, and 8.79% after four weeks. Dermal density was reportedly increased by 16.74% after two weeks, and 27.63% after four weeks.⁽⁷⁾

Palmitoyl Tetrapeptide-7 is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.

References

1. National Center for Biotechnology Information (2023). PubChem Compound Summary for CID 10078408, Palmitoyl tetrapeptide-7.
2. Mondon P, Hillion M, Peschard O, Andre N, Marchand T, Doridot E, Feuilloley MG, Pionneau C, Chardonnet S. Evaluation of dermal extracellular matrix and epidermal-dermal junction modifications using matrix-assisted laser desorption/ionization mass spectrometric imaging, in vivo reflectance confocal microscopy, echography, and histology: effect of age and peptide applications. J Cosmet Dermatol. 2015 Jun;14(2):152-60. doi: 10.1111/jocd.12135. Epub 2015 Mar 27. PMID: 25817264. https://pubmed.ncbi.nlm.nih.gov/25817264/
3. Sorsa T, Tjäderhane L, Salo T. Matrix metalloproteinases (MMPs) in oral diseases. Oral Dis. 2004 Nov;10(6):311-8. doi: 10.1111/j.1601-0825.2004.01038.x. PMID: 15533204. https://pubmed.ncbi.nlm.nih.gov/15533204/
4. Resende, Diana I S P et al. “Usage of Synthetic Peptides in Cosmetics for Sensitive Skin.” Pharmaceuticals (Basel, Switzerland) vol. 14,8 702. 21 Jul. 2021, doi:10.3390/ph14080702
5. Matrixyl 3000 (palmitoyl oligopeptide & palmitoyl tetrapeptide-7): Back to the future of skin care.
6. Marta Salvador-Ferreira et al. Trending Anti-Aging Peptides. MDPI Journal, Vol 7, Issue 4. https://www.mdpi.com/2079-9284/7/4/91
7. Hahn Hyung Jin et al. Instrumental evaluation of anti‑aging effects of cosmetic formulations containing palmitoyl peptides, Silybum marianum seed oil, vitamin E and other functional ingredients on aged human skin, Experimental and Therapeutic Medicine, Jun 2016.

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Nonapeptide-1

Nonapeptide-1 is a nine amino acid peptide that was first developed in the 1990s, sparking research interest due to its potential to inhibit the synthesis of melanin, the main pigment in mammals responsible for color in the skin, fur, hair, eyes, etc. The research on Nonapeptide-1 is still in its early stages, and much is still unknown about its potential and mechanisms of action.

Studies on Nonapeptide-1 have primarily focused on its potential to inhibit melanin production by interfering with the signaling pathway involved in melanogenesis. Specifically, Nonapeptide-1 is thought by researchers to possibly inhibit the melanocortin-1 receptors, which may prevent the action of melanocyte-stimulating hormones and the activation of the enzyme tyrosinase, which is necessary for the synthesis of melanin.⁽¹⁾ By doing so, Nonapeptide-1 may have a reducing potential on hyperpigmentation and skin tone in animal studies. Nevertheless, further studies are needed to fully understand the potential of this peptide.

Chemical Makeup

Molecular formula: C₆₁H₈₇N₁₅O₉S
Molecular weight: 1206.5 g/mol

Research and Clinical Studies

Nonapeptide-1 Discovery and Mechanism of Action

Scientists have investigated a peptide library of 31,360 structurally different melanocortin-1 receptor antagonists with the aim of finding the most potentially potent inhibitor of these receptors.⁽²⁾ These melanocortin-1 receptors may be found in melanocytes, which are pigment-producing cells. One of the main agonists of these receptors is considered to be the alpha-melanocyte-stimulating hormone (α-MSH).

α-MSH is a neuropeptide thought to be involved in regulating pigmentation, energy homeostasis, and immune function. The pituitary gland and the skin produce it. α-MSH may stimulate melanin production by binding to the melanocortin-1 receptor on melanocytes and activating a signaling cascade that increases tyrosinase activity and melanin production. Tyrosinase is the rate-limiting enzyme in melanogenesis.⁽³⁾ In addition, α-MSH may also act as an antagonist for the agouti signaling protein (ASP), which inhibits MC1R activity and reduces melanin production.

The researchers suggested that the most potent antagonist of all 31,360 peptides was Met-Pro-D-Phe-Arg-D-Trp-Phe-Lys-Pro-Val-NH2, aka nonapeptide-1.⁽²⁾ The scientists reported that it “has an IC50 value of 11 +/- 7 nM” and the “analysis revealed that D-Trp5 and Phe6 were crucial to its antagonistic properties which could be potentiated by D-Phe3.”

Nonapeptide-1 and Skin Pigmentation

The potential action of Nonapeptide-1 has been researched in both clinical and laboratory settings. In one in vitro study, keratinocyte cell line (HaCaT) cells and epidermal melanocytes (HEM) were exposed to UVA and imbued with different concentrations of the acetate salt of Nonapeptide-1.⁽⁴⁾

The scientists accessed cell viability, melanin content, and tyrosinase activity. The scientists suggested that Nonapeptide-1 downregulated melanocortin 1 receptor expression without affecting α-MSH levels, and might significantly decrease the expression of tyrosinase, TRP1 (tyrosinase-related protein-1), TRP2 (tyrosinase-related protein-2), and MITF (microphthalmia-associated transcription factor) with or without concomitant UVA radiation. Besides, the researchers further posited that cells infused with nonapeptide-1 may significantly increase the ability to resist melanin production.

More recent research on nonapeptide-1 also hypothesizes that the peptide may produce an apparent skin lightening by at least 33% and suggested a continued improvement over time.⁽⁵⁾ The only clinical trial on the topic was a prospective double-blinded parallel-group randomized controlled pilot study that lasted eight months and had three phases.⁽⁶⁾ The researchers reported an apparent improvement in severity scores of melasma and mean melanin index. They also commented, “The melasma area and severity index score showed a consistent reduction in the case group, whereas it increased in the control group from baseline.”

Nonapeptide-1 and Future Research Potential

Apart from melanocytes, the melanocortin 1 receptors that Nonapeptide-1 potentially inhibits may be expressed in other cells, such as nerve cells and immune cells. More specifically, the melanocortin 1 receptors may be found in the periaqueductal gray matter, which plays a major role in nociception.⁽⁷⁾

Scientists have conducted experiments on mice with overexpression of an endogenous antagonist of the melanocortin 1 receptor compared to control mice.⁽⁸⁾ They tested their response to painful and non-painful stimuli and their response to inflammatory and neuropathic pain. Additionally, they tested their aversion to capsaicin, which may activate the TRPV1 noxious heat receptor, using a paired preference paradigm.

The scientists indicated that mice overexpressing the melanocortin 1 receptor antagonist exhibited an apparently reduced inflammatory pain response and a slower onset of inflammation-induced hypersensitivity and allodynia. They were also observed to exhibit a decreased aversion to moderate concentrations of capsaicin. The scientists highlighted that these results occurred only in female mice and that “mice of either sex did not show any effect of mutant genotype on neuropathic pain.”

Studies also suggest that melanocortin 1 receptors may play a role in the growth and survival of melanoma tumor cells.⁽⁹⁾ Melanoma is a type of skin cancer with a high mortality rate, and mutations in the melanocortin 1 receptor gene may be associated with changes in the risk of developing melanoma. In this study, the researchers inhibited melanocortin 1 receptors using natural inhibitors, which reduced melanin synthesis and morphological heterogeneity in murine B16-F10 melanoma cells. They found that the inhibition resulted in slower tumor cell growth and a more homogeneous size and morphology of the tumors.

The study suggests that melanocortin 1 receptors may play an important role in regulating melanoma growth and morphology, and persistent inhibition of melanocortin 1 receptors may significantly slow the growth rate of the tumor cells that express these receptors. Nonapeptide-1 hasn’t been researched regarding its potential impact on melanoma tumor cells.

Nonapeptide-1 is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.

References:

1. Dhatt S (2006) Rebuilding the dermal matrix with this new in-demand ingredient in skin care products. Aesthetic Trends Technol 17–20
2. Jayawickreme, C. K., Quillan, J. M., Graminski, G. F., & Lerner, M. R. (1994). Discovery and structure-function analysis of alpha-melanocyte-stimulating hormone antagonists. Journal of Biological Chemistry, 269(47), 29846-29854.
3. Gaston, L. S., & Majzoub, J. A. (2022). Adrenocorticotrophin. In The Pituitary (pp. 51-89). Content Repository Only!.
4. Chen, J., Li, H., Liang, B., & Zhu, H. (2022). Effects of tea polyphenols on UVA-induced melanogenesis via inhibition of α-MSH-MC1R signalling pathway. Postepy dermatologii i alergologii, 39(2), 327–335. https://doi.org/10.5114/ada.2022.115890
5. Mohammed, Y. H., Moghimi, H. R., Yousef, S. A., Chandrasekaran, N. C., Bibi, C. R., Sukumar, S. C., Grice, J. E., Sakran, W., & Roberts, M. S. (2017). Efficacy, Safety and Targets in Transdermal Active and Excipient Delivery. Percutaneous Penetration Enhancers Drug Penetration Into/Through the Skin: Methodology and General Considerations, 369–391. https://doi.org/10.1007/978-3-662-53270-6_23
6. Chatterjee, M., Neema, S., & Rajput, G. R. (2021). A randomized controlled pilot study of a proprietary combination versus sunscreen in melasma maintenance. Indian journal of dermatology, venereology and leprology, 88(1), 51–58. https://doi.org/10.25259/IJDVL_976_18
7. Xia, Y., Wikberg, J. E., & Chhajlani, V. (1995). Expression of melanocortin 1 receptor in periaqueductal gray matter. Neuroreport, 6(16), 2193-2196.
8. Delaney, A., Keighren, M., Fleetwood-Walker, S. M., & Jackson, I. J. (2010). Involvement of the melanocortin-1 receptor in acute pain and pain of inflammatory but not neuropathic origin. PloS one, 5(9), e12498. https://doi.org/10.1371/journal.pone.0012498
9. Kansal, R. G., McCravy, M. S., Basham, J. H., Earl, J. A., McMurray, S. L., Starner, C. J., Whitt, M. A., & Albritton, L. M. (2016). Inhibition of melanocortin 1 receptor slows melanoma growth, reduces tumor heterogeneity and increases survival. Oncotarget, 7(18), 26331–26345. https://doi.org/10.18632/oncotarget.8372

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GHK-Cu is a naturally occurring complex molecule composed of a tripeptide called GHK (made up of glycine, histidine, and lysine amino acids) bound to a copper ion. The copper ion appears to stabilize and deliver GHK to cells. Research suggests that GHK-Cu may play a potentially essential role in restoring damaged tissues, wound repair, and may support immune response. These hypotheses have sprung from it’s perceived potential to stimulate the production of collagen, elastin, and glycosaminoglycans, crucial intercellular matrix components.

In addition to its potential on the intercellular matrix, GHK-Cu may also have antioxidant and anti-inflammatory characteristics that may protect cells from damage caused by free radicals.

Chemical Makeup

Molecular Formula: C₁₄H₂₃CuN₆O₄
Molecular Weight: 340.38 g/mol
Other Known Titles: Cu-GHK, Copper tripeptide-1, 6BJQ43T1I9

Research and Clinical Studies

GHK-Cu and Collagen Synthesis

Studies suggest that GHK-Cu may stimulate collagen synthesis and induce in situ tissue recovery. The researchers suggest that these actions may be due to “the presence of a GHK triplet in the alpha 2(I) chain of type I collagen”.⁽¹⁾ More specifically, the tripeptide sequence composed of glycine, histidine, and lysine, abbreviated as Gly-His-Lys, may be derived during the breakdown of collagen through hydrolysis. This breakdown is typically associated with the disintegration of collagen fibers, frequently resulting from either tissue damage or the natural degradation process. It is proposed that this specific peptide sequence may have a significant impact on cellular communication processes, specifically targeting fibroblasts. Fibroblasts are specialized cells deemed essential in producing new collagen fibers, vital components for structural support in various tissues.

The interaction between the Gly-His-Lys peptide and fibroblasts is believed to potentially initiate a cascade of biological events leading to the synthesis of collagen, thereby playing a potential role in the mechanisms of tissue repair and regeneration. This process of collagen synthesis by fibroblasts may be critical to contribute to the overall restoration and healing of damaged tissues. One study, lasted a month, reported that GHK-Cu might stimulate type 1 collagen production in clinical settings.⁽²⁾ The scientists compared the potential of GHK-Cu to other peptides and vitamin C and vitamin A derivatives on photodamaged skin. The research primarily investigated the potential action of the peptide on dermal procollagen synthesis, keratinocyte proliferation, differentiation, and cutaneous inflammation. The peptide appeared to improve all indicators, and the researchers reported an apparent increase in skin thickness, elasticity, and hydration.

Another study explored the potential interaction between GHK-Cu and hyaluronic acid (HA) on collagen synthesis, particularly focusing on their potential collaborative actions in dermal fibroblasts and an ex-vivo skin model.⁽³⁾ HA is portrayed as a significant component of skin cells, noted for its moisture-binding potential and actions on cell proliferation and inflammation, with different molecular weights (LMW and HMW) showing distinct biological activities. The experimental setup involved exposure of dermal fibroblasts with various combinations of GHK-Cu and HA, measuring the synthesis of collagen types I, IV, and VII. It was suggested that certain combinations, particularly at a GHK-Cu to LMW HA ratio of 1:9, appeared to have significantly boosted the synthesis of collagen IV—more so than when either compound was studied independently. This suggests a potential synergistic action between GHK-Cu and HA, specifically in enhancing collagen IV levels. The synergy might arise from the combined action of GHK-Cu in stimulating glycosaminoglycan production, promoting collagen synthesis, and HA’s role in reducing collagen degradation by scavenging reactive oxygen species and inhibiting matrix metalloproteinases. The research highlights that the molecular weight of HA and the ratio of GHK-Cu to HA may be crucial in maximizing this action, with optimal results observed at specific ratios. Further studies employing an ex-vivo skin model supported these findings, suggesting a notable increase in collagen IV synthesis at the dermal-epidermal junction when exposed to the optimized GHK-Cu and LMW HA mixture. This action was visually corroborated through increased fluorescence intensity in immunofluorescence assays, indicating higher collagen IV content.

GHK-Cu and Wound Infection

Both animal and clinical studies have hypothesized that GHK-Cu may reduce inflammation and the risk of infection in wounds. One murine study investigated the potential of GHK-Cu on ischemic open wounds.⁽⁴⁾ The researchers reported, “On days 6, 10, and 13, tripeptide-copper complex-treated wounds contained significantly lower concentrations of TNF-alpha and MMP-2 and MMP-9 than control wounds.” Tumor necrosis factor-alpha (TNF-alpha), a cytokine involved in systemic inflammation, along with matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) — enzymes that break down extracellular matrix proteins — might potentially influence both the inflammatory processes and the remodeling of tissues. This suggests that GHK-Cu, a copper complex recognized for its healing capacities, might have a role in reducing inflammation and preventing tissue breakdown in models of ischemic wounds, where blood flow restriction potentially causes tissue damage.

A clinical trial that involved GHK-Cu in addition to standard wound care also reported an apparently reduced risk of infection compared to standard processes alone.⁽⁵⁾ The study was conducted on models of diabetic neuropathic ulcers, and the rate of infections was only 7% in the GHK-Cu models compared to 34% in the control models.

GHK-Cu and Wound Healing

Studies in rabbits report that GHK-Cu has been tested regarding its potential in wound healing and laser exposure at different intensities.⁽⁶⁾ The results were compared to control wounds without intervention. Wounds were observed daily, and biopsies were taken weekly for four weeks to evaluate the inflammation rate and neovascularization. The GHK-Cu and high-intensity laser groups appeared to have a shorter average time for healing and greater neutrophil and vessel counts. There was an apparently shorter median time for the first observable granulation tissue and an apparently faster filling of an open wound with granulation tissue compared to the control group. Granular tissue is composed of newly formed connective tissue and minuscule blood vessels that appear on wound surfaces as part of the healing process. It is suggested that there might be a link between the emergence of this tissue and heightened activity of antioxidant enzymes. These enzymes are proteins that assist in shielding cells from the harmful action of oxidative stress, a process where cell components are damaged due to the presence of unstable molecules known as free radicals. Furthermore, there is a potential enhancement in vascular development observed in these scenarios. This vascular development is considered vital for transporting essential nutrients and oxygen to the damaged area, thereby facilitating the repair of tissue.

The previously mentioned study on rats with open ischemic wounds also reported an apparent decrease in wound area of the GHK-Cu group that was greater compared to the control group on days 3 to 5, 6 to 9, and 11 to 13.⁽⁴⁾

Similarly, the clinical study on models of diabetic neuropathic ulcers reported that GHK-Cu, combined with standard wound care, appeared more impactful for wound closure than standard care alone.⁽⁵⁾ The apparent closure rate was three times faster than standard care. The researchers also suggested that “The enhancement of wound closure was more pronounced (median of 89.2% compared with -10.3% for vehicle; p < 0.01) in larger (greater than 100 mm(2) initial area at study entry) plantar ulcers caused by the failure of this size of ulcer to respond adequately to standardized wound care.”

In research involving both standard murine models and those adapted to mimic diabetic conditions, wound dressings composed of collagen and infused with GHK were observed to potentially enhance wound healing.⁽⁷⁾ The observations suggest that by the conclusion of the third week, wounds exposed to dressings containing biotinylated GHK (a tripeptide with skin regenerative properties) nearly achieved full closure, registering at 99.39%. This is potentially a significant enhancement compared to the 69.49% closure rate observed with control dressings lacking this modification. Further analysis indicated that the wounds exposed to GHK might have shown elevated levels of glutathione and ascorbic acid. These are considered critical antioxidants for their potential roles in facilitating tissue repair by protecting cells from oxidative stress. There was also a tentative observation of increased epithelialization, a process essential for the regeneration of the skin’s outer layer, in these experimental conditions. Apart from the enhanced activity of fibroblasts, which are pivotal in collagen synthesis, tissue repair, and regeneration, there was also noted a potential rise in mast cell activation. Mast cells are important for mediating inflammatory responses, which are deemed crucial during the initial phases of wound healing.

GHK-Cu and Active Radicals

Photodamage of tissues such as the skin involves the formation of reactive oxygen species (ROS), reactive nitrogen species (RNS), and reactive carbonyl species (RCS), which may induce damage to proteins, DNA, and lipids. Studies suggest that the amino acid sequence in GHK-Cu may have anti-RCS potential against radicals such as 4-hydroxynoneal, acrolein, malondialdehyde, and others.⁽⁸⁾ Furthermore, it may potentially prevent protein glycation. Moreover, researchers have suggested that GHK-Cu may have potential action in reducing iron release from ferritin. Ferritin is a lipid peroxidation catalyst, and GHK-Cu may help to reduce the formation of iron complexes in damaged tissues and thus decrease inflammation. One study suggested an 87% decrease in iron release with the help of GHK-Cu to lower oxidation in damaged tissues.⁽⁹⁾

GHK-Cu may also reduce the production of reactive oxygen species and inflammatory cytokines while increasing the activity of antioxidant enzymes. This was proposed by an animal study investigating the potential of GHK-Cu on lipopolysaccharide-induced lung inflammation in mice.⁽¹⁰⁾ The peptide was suggested to suppress the activation of NF-κB and p38 MAPK signaling pathways associated with inflammation. This might potentially lead to reduced infiltration of inflammatory cells in the lungs of mice with lung damage and lower levels of TNF-1 and IL-6 production to minimize damage.

Further studies also suggest that the amino-acid sequence of GHK-Cu may have an antioxidative potential on ROS, such as hydroxyl radicals, and it may be even stronger than generic antioxidative peptides.⁽¹²⁾

GHK-Cu and Wrinkles in Skin Tissue Models

GHK-Cu has been suggested to host potential for improving experimental models of disturbed skin topography, such as wrinkles and fine lines. One study posited that a GHK-Cu possibly reduces visible bioindicators, improving skin laxity, and clarity. The peptide apparently also reduced the depth of wrinkles while potentially increasing skin density and thickness after 12 weeks of experimentation in skin cell models with varying degrees of photodamage.⁽¹³⁾

Another investigation focused on the actions of GHK-Cu compared to a control compound and vitamin K. Over a period of 12 weeks, the GHK-Cu ostensibly performed better than the controls in reducing epidermal wrinkles. The peptide may also have increased skin density and thickness.⁽¹⁴⁾

In a separate 12-week study in mild to advanced photodamage, GHK-Cu seemingly improved skin attributes such as laxity, clarity, and firmness. This peptide was also associated with a reduction in coarse wrinkles, and mottled pigmentation. Additionally, the peptide apparently stimulated dermal keratinocyte proliferation, as evidenced by histological analysis of biopsies.⁽¹⁵⁾

GHK-Cu peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.

References

1. Maquart, F. X., Pickart, L., Laurent, M., Gillery, P., Monboisse, J. C., & Borel, J. P. (1988). Stimulation of collagen synthesis in fibroblast cultures by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+. FEBS letters, 238(2), 343–346. https://doi.org/10.1016/0014-5793(88)80509-x
2. Abdulghani, A. A., Sherr, A., Shirin, S., Solodkina, G., Tapia, E. M., Wolf, B., & Gottlieb, A. B. (1998). Effects of creams containing vitamin C, a copper-binding peptide cream and melatonin compared with tretinoin on the ultrastructure of normal skin-A pilot clinical, histologic, and ultrastructural study. Disease Management and Clinical Outcomes, 4(1), 136-141.
3. Jiang F, Wu Y, Liu Z, Hong M, Huang Y. Synergy of GHK-Cu and hyaluronic acid on collagen IV upregulation via fibroblast and ex-vivo skin tests. J Cosmet Dermatol. 2023 Sep;22(9):2598-2604. doi: 10.1111/jocd.15763. Epub 2023 Apr 16. PMID: 37062921.
4. Canapp, S. O., Jr, Farese, J. P., Schultz, G. S., Gowda, S., Ishak, A. M., Swaim, S. F., Vangilder, J., Lee-Ambrose, L., & Martin, F. G. (2003). The effect of tripeptide-copper complex on healing of ischemic open wounds. Veterinary surgery : VS, 32(6), 515–523. https://doi.org/10.1111/j.1532-950x.2003.00515.x
5. Mulder, G. D., Patt, L. M., Sanders, L., Rosenstock, J., Altman, M. I., Hanley, M. E., & Duncan, G. W. (1994). Enhanced healing of ulcers in patients with diabetes by treatment with glycyl-l-histidyl-l-lysine copper. Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society, 2(4), 259–269. https://doi.org/10.1046/j.1524-475X.1994.20406.x
6. Gul, N. Y., Topal, A., Cangul, I. T., & Yanik, K. (2008). The effects of tripeptide copper complex and helium-neon laser on wound healing in rabbits. Veterinary dermatology, 19(1), 7–14. https://doi.org/10.1111/j.1365-3164.2007.00647.x
7. Alven, S., Peter, S., Mbese, Z., & Aderibigbe, B. A. (2022). Polymer-Based Wound Dressing Materials Loaded with Bioactive Agents: Potential Materials for the Treatment of Diabetic Wounds. Polymers, 14(4), 724. https://doi.org/10.3390/polym14040724
8. Cebrián, J., Messeguer, A., Facino, R. M., & García Antón, J. M. (2005). New anti-RNS and -RCS products for cosmetic treatment. International journal of cosmetic science, 27(5), 271–278. https://doi.org/10.1111/j.1467-2494.2005.00279.x
9. Miller, D. M., DeSilva, D., Pickart, L., & Aust, S. D. (1990). Effects of glycyl-histidyl-lysyl chelated Cu(II) on ferritin dependent lipid peroxidation. Advances in experimental medicine and biology, 264, 79–84. https://doi.org/10.1007/978-1-4684-5730-8_11
10. Park, J. R., Lee, H., Kim, S. I., & Yang, S. R. (2016). The tri-peptide GHK-Cu complex ameliorates lipopolysaccharide-induced acute lung injury in mice. Oncotarget, 7(36), 58405–58417. https://doi.org/10.18632/oncotarget.11168
11. Zhang, Q., Yan, L., Lu, J., & Zhou, X. (2022). Glycyl-L-histidyl-L-lysine-Cu2+ attenuates cigarette smoke-induced pulmonary emphysema and inflammation by reducing oxidative stress pathway. Frontiers in molecular biosciences, 9, 925700. https://doi.org/10.3389/fmolb.2022.925700
12. Sakuma, S., Ishimura, M., Yuba, Y., Itoh, Y., & Fujimoto, Y. (2018). The peptide glycyl-ʟ-histidyl-ʟ-lysine is an endogenous antioxidant in living organisms, possibly by diminishing hydroxyl and peroxyl radicals. International journal of physiology, pathophysiology and pharmacology, 10(3), 132–138.
13. Leyden J., Stephens T., Finkey M., Appa Y., Barkovic S. Skin care benefits of copper peptide containing facial cream. Proceedings of the American Academy of Dermatology Meeting; February 2002; New York, NY, USA.
14. Leyden J., Stephens T., Finkey M., Barkovic S. Skin Care Benefits of Copper Peptide Containing Eye Creams. University of Pennsylvania; 2002.
15. Finkley M., Appa Y., Bhandarkar S. Copper peptide and skin. In: Elsner P., Maibach H., editors. Cosmeceuticals and Active Cosmetics: Drugs vs. Cosmetics. New York, NY, USA: Marcel Dekker; 2005. pp. 549–563.

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Research Acetyl Hexapeptide-3 (Argireline) (200mg) For Sale

All products are sold for research, laboratory, or analytical purposes only, and are not for human consumption.

Core Peptides is a chemical supplier. Core Peptides is not a compounding pharmacy or chemical compounding facility as defined under 503A of the Federal Food, Drug, and Cosmetic act. Core Peptides is not an outsourcing facility as defined under 503B of the Federal Food, Drug, and Cosmetic act.

The statements made within this website have not been evaluated by the US Food and Drug Administration. The products we offer are not intended to diagnose, treat, cure or prevent any disease.

Human/Animal Consumption Prohibited. Laboratory/In-Vitro Experimental Use Only

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Tripeptide-29

Tripeptide-29 is a small, naturally occurring amino-acid peptide, one of the primary building blocks for collagen protein.⁽¹⁾ Collagen is a major component of the extracellular matrix, the network of proteins and fibers comprising connective tissues. It is considered responsible for providing structure and support to cellular complexes.

Researchers suggest Tripeptide-29 may have the potential to stimulate collagen synthesis and promote the formation of collagen fibers. In addition to its possible role in collagen synthesis, Tripeptide-29 may have other biological functions. For example, research studies have hypothesized its potential as an antioxidant, which might help protect cells from oxidative stress and damage. It may also exhibit anti-inflammatory, anti-fibrotic, and anti-melanogenic characteristics.

Chemical Makeup

Molecular Formula: C₁₂H₁₉N₃O₅
Molecular Weight: 285.3 g/mol
Other Known Titles: Glycylprolylhydroxyproline

Research and Clinical Studies

Tripeptide-29 and Collagen Integrity

Tripeptide-29 may be a major contributor to the stability of type 1 collagen molecules. Studies suggest that the OH group of Hyp in Tripeptide-29 may contribute to the formation of favorable interatomic interactions.⁽²⁾ The researchers propose that Tripeptide-29 as a monomer may enhance the stability of collagen and collagen microfibrils. Studies also suggest that the presence of Tripeptide-29 as a part of the sequence in collagen may significantly reduce UV-related damage and lower the degradation rate when exposed to intensive radiation.⁽³⁾

A study conducted on dermal fibroblasts reported that hydrolyzed type 1 collagen tripeptides exhibited promising potential in reducing oxidative stress and damage.⁽⁴⁾ As previously noted, Tripeptide-29 appears to be the primary tripeptide that forms when hydrolyzing type 1 collagen. The hydrolysate showed potential in reducing the build-up of advanced glycation end products (AGEs), reportedly preventing the production of denatured collagen and lowering levels of reactive oxygen species. The glycation process refers to sugar molecules bonding with proteins, potentially speeding up skin cell aging by altering its mechanical properties and stability. Ultimately, the scientists suggested that tripeptide-29 “might improve [cell aging] phenotypes via the inhibition of glycation and oxidative stress, leading to a delay in cellular aging.” From an in vitro perspective, the study explored the mechanisms underpinning the observed action. It was suggested that Tripeptide-29 may reduce the production of AGEs and denatured collagen while inhibiting the activity of matrix metalloproteinases (MMPs) and enhancing collagen 1 levels in dermal fibroblasts. These results suggest that Tripeptide-29 may mitigate cell aging by preserving collagen integrity and inhibiting processes that degrade the skin matrix. Furthermore, it is indicated that Tripeptide-29 might be linked to its smaller peptide size, which is believed to support its skin penetration and bioavailability.

Tripeptide-29 and Glucose Control

According to researchers, Tripeptide-29 may act as a peptidic inhibitor of dipeptidyl peptidase-IV (DPP-IV) due to its potential to inhibit the hydrolysis of the Pro-Hyp bond.⁽⁵⁾ It was considered a moderately competitive inhibitor. The scientists reported that “Gly-Pro-Hyp in the collagen hydrolysates is suggested to be mainly responsible for the DPP-IV inhibition in vitro,” inferring that Tripeptide-29 may contribute to the overall inhibitory action of collagen peptides on DPP-IV. Interestingly, Tripeptide-29 was reportedly not hydrolyzed by DPP-IV, indicating resistance to this specific enzyme. This observation might point to the peptide’s stability and efficacy in the presence of this enzyme.

Dipeptidyl peptidase-IV (DPP-IV) is a serine peptidase involved in several biological processes.⁽⁶⁾ The enzyme is expressed on the surface of various cell types, including immune cells, epithelial cells, and endothelial cells. It is also apparently found in circulation in the liver, kidney, and intestine tissues. DPP-IV cleaves peptide bonds at the N-terminus of dipeptides, tripeptides, and smaller peptides, but not larger peptides or proteins. This specificity means it may act on various substrates, including hormones, neuropeptides, and chemokines. Some of the substrates of DPP-IV include glucagon-like peptide-1 (GLP-1), glucose-dependent insulinotropic polypeptide (GIP), and peptide YY (PYY), all of which are suggested to be involved in the regulation of glucose homeostasis and energy metabolism.⁽⁷⁾ The cleavage of GLP-1 and GIP by DPP-IV may result in rapid inactivation and clearance from circulation. Inhibiting DPP-IV may upregulate the levels of GLP-1 and GIP, which may lead to an increase in insulin secretion, reduction in glucagon levels, lower blood glucose, and decreased appetite.⁽⁸⁾

Tripeptide-29 and Platelet Aggregation

Collagen-related peptides that contain a glycine-proline-hydroxyproline repeat motif are considered to be cross-linked through cysteine residues, which may stimulate platelet aggregation and secretion through glycoprotein VI (GPVI) receptors. GPVI is a platelet receptor that scientists believe to be crucial in blood clotting or hemostasis. It is a transmembrane glycoprotein that appears to be primarily expressed on the surface of platelets, which are blood cells involved in blood clotting. GPVI is a member of the immunoglobulin (Ig) superfamily of proteins, comprised of two subunits called alpha and beta. The alpha subunit is considered to contain the collagen-binding site, while the beta subunit is deemed responsible for signaling within the platelet. When the GPVI receptor binds to collagen, it may trigger a series of events that lead to the activation of platelets and the formation of a blood clot.

Studies suggest that the non-cross-linked form of glycine-proline-hydroxyproline, or Tripeptide-29, may induce tyrosine phosphorylation of the tyrosine kinase Syk and phospholipase C gamma2 (PLCgamma2) in platelets.⁽⁹⁾ This may ultimately stimulate platelet aggregation to stop or prevent bleeding. Overall, the researchers report that Tripeptide-29, “present as a repeat motif, is sufficient to activate the platelet collagen receptor GPVI,” and may stimulate the formation of thrombi to prevent excessive bleeding.

Tripeptide-29 peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.

References:

1. Wiśniewski, K., Artemowicz, B., Lutostańska, A., Maćkowiak, J., & Koziołkiewicz, W. (1994). Central activity of peptide Gly-Pro-Hyp–the main component of collagen degradation products mixture. Acta neurobiologiae experimentalis, 54(1), 33–38.
2. Némethy, G., & Scheraga, H. A. (1986). Stabilization of collagen fibrils by hydroxyproline. Biochemistry, 25(11), 3184–3188. target=”_blank” rel=”noopener”https://doi.org/10.1021/bi00359a016
3. Jariashvili, K., Madhan, B., Brodsky, B., Kuchava, A., Namicheishvili, L., & Metreveli, N. (2012). UV damage of collagen: insights from model collagen peptides. Biopolymers, 97(3), 189–198. https://doi.org/10.1002/bip.21725
4. Lee, Y. I., Lee, S. G., Jung, I., Suk, J., Lee, M. H., Kim, D. U., & Lee, J. H. (2022). Effect of a Collagen Tripeptide on Antiaging and Inhibition of Glycation of the Skin: A Pilot Study. International journal of molecular sciences, 23(3), 1101. https://doi.org/10.3390/ijms23031101
5. Hatanaka, T., Kawakami, K., & Uraji, M. (2014). Inhibitory effect of collagen-derived tripeptides on dipeptidylpeptidase-IV activity. Journal of enzyme inhibition and medicinal chemistry, 29(6), 823–828. https://doi.org/10.3109/14756366.2013.858143
6. Trzaskalski, N. A., Fadzeyeva, E., & Mulvihill, E. E. (2020). Dipeptidyl Peptidase-4 at the Interface Between Inflammation and Metabolism. Clinical medicine insights. Endocrinology and diabetes, 13, 1179551420912972. https://doi.org/10.1177/1179551420912972
7. Kieffer, T. J., McIntosh, C. H., & Pederson, R. A. (1995). Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology, 136(8), 3585–3596. https://doi.org/10.1210/endo.136.8.7628397
8. Kasina, S. V. S. K., & Baradhi, K. M. (2022). Dipeptidyl Peptidase IV (DPP IV) Inhibitors. In StatPearls. StatPearls Publishing.
9. Asselin, J., Knight, C. G., Farndale, R. W., Barnes, M. J., & Watson, S. P. (1999). Monomeric (glycine-proline-hydroxyproline)10 repeat sequence is a partial agonist of the platelet collagen receptor glycoprotein VI. The Biochemical journal, 339 ( Pt 2)(Pt 2), 413–418.

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Syn-Coll Peptide

Syn-Coll is a synthetic peptide compound, also known as palmitoyl tripeptide-5. It was designed to mimic the activity of thrombospondin-1 (TSP-1), a natural extracellular matrix protein that apparently stimulates transforming growth factor beta (TGF-β). TGF-β is a crucial growth factor that plays a vital role in maintaining skin integrity and stimulating the postnatal development of skin structures by promoting collagen synthesis.

The short sequence Lys-Arg-Phe-Lys of TSP-1 is considered responsible for TGF-β stimulation.⁽¹⁾ Syn-Coll has the sequence of Palmitoyl-Lys-Val-Lys, and scientists report that it may exert similar action on TGF-β. As a result, animal models and dermal fibroblasts cell culture tests suggest it may stimulate collagen production. More specifically, Syn-Coll may increase the production of Type I and Type III collagen by dermal fibroblasts via stimulating TGF-β activity.

Furthermore, Syn-Coll has been extensively studied in animal models and experiments, which all generally hypothesize that it exhibits some potential to increase collagen synthesis but also prevent collagen degradation. Syn-Coll may prevent collagen breakdown by inhibiting the activity of matrix metalloproteinases (MMPs) such as MMP1 and MMP3.

Chemical Makeup

Molecular Formula: C₃₃H₆₅N₅O₅
Molecular Weight: 611.9 g/mol
Other Known Titles: Palmitoyl-lysyl-valyl-lysine, Palmitoyl Tripeptide-5

Research and Clinical Studies

Syn-Coll Peptide and Collagen Synthesis

Collagen is a major component of the extracellular matrix, the network of proteins and fibers that comprise dermal connective tissue.
Recent studies have indicated that Syn-Coll may stimulate collagen synthesis. This synthetic peptide is believed to work by mimicking the activity of TSP-1 to activate the growth factor TGF-β. More specifically, Syn-Coll may work by mimicking part of the sequence of TSP-1.⁽²⁾

TGF-β is a crucial growth factor that has been suggested to play an important role in regulating collagen production. Studies have suggested that Syn-Coll works by activating latent TGF-β, thereby increasing the production of type I and type III collagen by dermal fibroblasts. As a result, scientists report that activating TGF-β “causes a persistent increase in steady-state amounts of type I and type III collagen and fibronectin mRNAs in normal […] dermal fibroblasts.“⁽³⁾

Trials have also indicated that Syn-Coll may increase type 1 collagen synthesis via TGF-β to a greater degree than other peptides, such as palmitoyl pentapeptide.⁽⁴⁾ The researchers posited that “Palmitoyl tripeptide-5 also known as Syn-Coll, increases collagen 1 production via TGF-b reportedly 60% more effective than palmitoyl pentapeptide.”

Syn-Coll Peptide and Collagen Breakdown

Matrix metalloproteinases (MMPs) are a group of enzymes involved in the degradation of extracellular matrix proteins, including collagen. Scientists consider MMPs to be typically produced by dermal cells, such as fibroblasts, and are involved in tissue remodeling and maintaining the extracellular matrix. However, they further posit when MMPs are overproduced or become dysregulated, they can contribute to dermal collagen breakdown. For example, MMP-1 is considered to be an enzyme that specifically degrades type I collagen.

Fibroblasts produce MMP-1, and its activity may be increased by factors such as UV radiation, inflammation, and oxidative stress. Another member of the MMPs is MMP-3, and considered capable of cleaving a wide range of extracellular matrix proteins, including collagens, laminin, fibronectin, proteoglycans, and elastin. It may be particularly active at degrading type II collagen, the main structural component of cartilage. MMP-3 has also been implicated in the degradation of other collagens, such as type III collagen, which is abundant in the skin and blood vessels.

Syn-Coll (Palmitoyl tripeptide-5) seems to decrease collagen breakdown by inhibiting matrix metalloproteinases degrading collagen. More specifically, studies suggest that Syn-Coll (palmitoyl tripeptide-5) may prevent collagen breakdown by interfering with MMP1 and MMP3 collagen degradation.⁽⁵⁾

Syn-Coll Peptide and Anti-Aging

Studies have suggested that Syn-Coll may reduce the appearance of wrinkles to a much greater extent than a placebo.⁽⁶⁾ The scientists reported that “formulation demonstrated a dose-dependent wrinkle reduction, measured by PRIMOS surface topography.” Ultimately, they concluded that Syn-Coll (palmitoyl tripeptide-5) might exhibit roughly 3.5 times the potential to reduce the appearance of wrinkles than the placebo. One study in 60 test subjects that lasted 84 days reported that Syn-Coll twice daily suggested it may exhibit anti-wrinkle potential and reduce skin roughness better than control groups, placebo, and other peptides.⁽⁷⁾ The peptide appeared to reduce wrinkle parameters by 12%.

Besides its potential on collagen synthesis and degradation, scientists suggest that Syn-Coll may exert possible anti-wrinkle action through other mechanisms.⁽⁸⁾ These include supporting the skin’s barrier function by possibly preventing water loss from the skin’s surface. This can help to maintain optimal hydration levels in the skin. Furthermore, Syn-Coll may act as a humectant, which can help absorb and retain water in the skin. It may also increase skin surface lipids and act as an emollient, providing partial occlusion, lubrication, and moisturization to the skin.

In addition, Syn-Coll may also be modified by adding an L-ascorbate moiety (AA) at the C-terminus (Pal-KVK-AA), which may have a depigmentation impact. Studies have suggested that this conjugation may inhibit melanin synthesis.⁽⁹⁾ By blocking melanin production, this modified version of Syn-Coll may help reduce hyperpigmentation caused by photoaging, UV light, oxidative stress, and other factors.

Syn-Coll peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.

References:

1. Murphy-Ullrich, J. E., & Poczatek, M. (2000). Activation of latent TGF-beta by thrombospondin-1: mechanisms and physiology. Cytokine & growth factor reviews, 11(1-2), 59–69. https://doi.org/10.1016/s1359-6101(99)00029-5
2. Trookman, N. S., Rizer, R. L., Ford, R., Ho, E., & Gotz, V. (2009). Immediate and Long-term Clinical Benefits of a Treatment for Facial Lines and Wrinkles. The Journal of clinical and aesthetic dermatology, 2(3), 38–43.
3. Varga, J., Rosenbloom, J., & Jimenez, S. A. (1987). Transforming growth factor beta (TGF beta) causes a persistent increase in steady-state amounts of type I and type III collagen and fibronectin mRNAs in normal human dermal fibroblasts. The Biochemical journal, 247(3), 597–604. https://doi.org/10.1042/bj2470597
4. Bucay, V. W., & Day, D. (2013). Adjunctive skin care of the brow and periorbital region. Clinics in plastic surgery, 40(1), 225–236. https://doi.org/10.1016/j.cps.2012.09.003
5. Errante, F., Ledwoń, P., Latajka, R., Rovero, P., & Papini, A. M. (2020). Cosmeceutical Peptides in the Framework of Sustainable Wellness Economy. Frontiers in chemistry, 8, 572923. https://doi.org/10.3389/fchem.2020.572923
6. Gorouhi, F., & Maibach, H. I. (2009). Role of peptides in preventing or treating aged skin. International journal of cosmetic science, 31(5), 327–345. https://doi.org/10.1111/j.1468-2494.2009.00490.x
7. Schneider, A. L. (2010). Evaluation of the penetration and efficacy of anti-aging compounds (Doctoral dissertation, Monash University).
8. Kim, H. M., An, H. S., Bae, J. S., Kim, J. Y., Choi, C. H., Kim, J. Y., Lim, J. H., Choi, J. H., Song, H., Moon, S. H., Park, Y. J., Chang, S. J., & Choi, S. Y. (2017). Effects of palmitoyl-KVK-L-ascorbic acid on skin wrinkles and pigmentation. Archives of dermatological research, 309(5), 397–402. https://doi.org/10.1007/s00403-017-1731-6

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Vialox Peptide

Vialox, or pentapeptide-3, is a synthetic peptide molecule with the amino acid sequence GPRPA. It is believed to work by blocking neuronal nicotinic acetylcholine receptors located in the postsynaptic membrane of muscle cells. These receptors transmit signals from nerve cells to muscle cells, resulting in muscle contraction. By potentially reducing the release of acetylcholine, Vialox may relax muscles, reducing wrinkle depth and development along the skin barrier. The mechanism of action of Vialox may be similar to that of tubocurarine, a natural alkaloid compound considered to have muscle-relaxing activity.

Chemical Makeup

Molecular Formula: C₂₁H₃₇N₉O₅
Molecular Weight: 495.58 g/mol
Other Known Titles: Pentapeptide-3V, SCHEMBL1552457, HY-P0099, ZINC35922739

Research and Clinical Studies

Vialox Peptide Mechanism of Action

Vialox is a synthetic peptide molecule suggested by researchers to be an inhibitor of neurotransmitter activity.⁽¹⁾ Vialox may act in a manner that is similar to that of tubocurarine, specifically through its interaction with acetylcholine receptors located on the postsynaptic membrane of muscle cells.⁽²⁾ Tubocurarine is a naturally occurring alkaloid compound found in the bark of certain plants, particularly in the species Chondrodendron tomentosum, commonly known as “curare.” It is considered to be a potent neurotoxin that appears to act as a non-depolarizing neuromuscular blocker by blocking the action of acetylcholine at the neuromuscular junction, thereby preventing muscle contraction.

Researchers also classify Vialox as a non-depolarizing neuromuscular blocker. The peptide appears to bind to the acetylcholine receptors on the postsynaptic membrane of muscle cells. By doing so, studies report that it acts as “a competitive antagonist at the acetylcholine postsynaptic membrane receptor.“⁽³⁾

The peptide may possibly interact with the neuronal nicotinic acetylcholine receptors. Nicotinic acetylcholine receptors reportedly play a crucial role in regulating muscle contraction by serving as the primary receptor in muscles for the communication between motor nerves and muscles at the neuromuscular junction.

As an antagonist, Vialox appears to block the binding of acetylcholine to these receptor sites, thereby preventing the opening of the sodium ion channels responsible for depolarizing the cell and normally leading to muscle contraction.⁽⁴⁾ By inhibiting the activity of the acetylcholine receptors, Vialox may cause the smooth muscles to stay relaxed, reducing wrinkles and fine lines in the skin.

Vialox Peptide and Wrinkle Development, Skin Texture

Vialox has been researched for its potential to reduce wrinkles upon the skin surface, and decrease texture variations along the skin barrier. There are some risks associated with using compounds to induce wrinkle reduction, particularly when used in higher concentrations or for extended periods. Furthermore, there is some concern that long-term exposure may have unknown or unanticipated impact. However, Vialox appears to have a short half-life and may be introduced less invasively. Nevertheless, it may be impactful, as researchers report that “studies […] showed that this [compound] softened wrinkles and reduced skin roughness⁽⁴⁾.

These researchers reported that the tests appeared to result in reduced muscle contractions by 71% within one minute after Vialox presentation, leading to a 58% reduction two hours later. Ultimately, the scientists suggested that the reduced frequency of muscle contractions has the potential to result in shallower lines along the surface of the skin barrier.

According to research, the peptide may also potentially mitigate the impact of skin wrinkles.⁽⁹⁾ The results of the study indicate a noticeable decrease of 49% in the size of wrinkles, accompanied by a 47% decrease in the roughness of the skin within a time frame of 28 days of consistent presentation.

Vialox peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.

References:

1. Husein el Hadmed, H., & Castillo, R. F. (2016). Cosmeceuticals: peptides, proteins, and growth factors. Journal of cosmetic dermatology, 15(4), 514-519.
2. Lupo, M. P., & Cole, A. L. (2007). Cosmeceutical peptides. Dermatologic therapy, 20(5), 343-349.
3. Gorouhi, F., & Maibach, H. I. (2009). Role of peptides in preventing or treating aged skin. International journal of cosmetic science, 31(5), 327-345.
4. Satriyasa B. K. (2019). Botulinum toxin (Botox) A for reducing the appearance of facial wrinkles: a literature review of clinical use and pharmacological aspect. Clinical, cosmetic and investigational dermatology, 12, 223–228. https://doi.org/10.2147/CCID.S202919
5. Kalandakanond, S., & Coffield, J. A. (2001). Cleavage of SNAP-25 by botulinum toxin type A requires receptor-mediated endocytosis, pH-dependent translocation, and zinc. The Journal of pharmacology and experimental therapeutics, 296(3), 980–986.
6. Bakheit A. M. (2006). The possible adverse effects of intramuscular botulinum toxin injections and their management. Current drug safety, 1(3), 271–279. https://doi.org/10.2174/157488606777934431
7. Witmanowski, H., & Błochowiak, K. (2020). The whole truth about botulinum toxin – a review. Postepy dermatologii i alergologii, 37(6), 853–861. https://doi.org/10.5114/ada.2019.82795
8. Reddy, B. Y., Jow, T., & Hantash, B. M. (2012). Bioactive oligopeptides in dermatology: Part II. Experimental dermatology, 21(8), 569-575.

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Decapeptide-12

Decapeptide-12 is a synthetic peptide that is composed of 10 amino acids. Its developers and subsequent researchers have suggested that Decapeptide-12 may potentially inhibit melanin production in the skin by suppressing the activity of tyrosinase, an enzyme involved in the synthesis of melanin.

Decapeptide-12 does not appear to mimic any naturally occurring peptide. Rather, it was designed and synthesized to exhibit specific properties. Decapeptide-12 is primarily researched in reducing melanin production and hyperpigmentation. It has also been studied for its potential impact on cell growth, differentiation, and mitigating cell aging. However, more research is needed to fully understand the potential properties and results of Decapeptide-12 experiments in these contexts.

Chemical Makeup

Molecular Formula: C₆₅H₉₀N₁₈O₁₇
Molecular Weight: 1311.46 g/mol

Overview and Mechanisms of Action

As mentioned, Decapeptide-12 is posited to work primarily by inhibiting melanin synthesis, aka melanogenesis. Melanin synthesis is suggested to be a complex biochemical pathway that may occur within specialized cells in the skin called melanocytes. Tyrosinase is posited to play a pivotal role in this pathway as it appears to catalyze the first two steps in melanin production: the hydroxylation of tyrosine to DOPA (3,4-dihydroxyphenylalanine) and the oxidation of DOPA to DOPAquinone. These reactions are suggested to be essential for the subsequent production of eumelanin and pheomelanin, the two main types of melanin pigments that determine skin, hair, and eye color and may protect against UV radiation. As mentioned, Decapeptide-12 may act by potentially inhibiting tyrosinase activity. While the precise molecular mechanisms are complex and involve multiple pathways, the basic understanding is that Decapeptide-12 may bind to specific sites on the tyrosinase enzyme or its mRNA, thereby blocking the enzyme’s ability to catalyze the aforementioned critical reactions in melanin synthesis. This inhibition could occur through direct interaction with the enzyme, leading to a change in its conformation and reducing its catalytic efficiency. Alternatively, Decapeptide-12 might interfere with the enzyme’s gene expression, lowering the amount of functional tyrosinase produced in the melanocytes.

Research and Clinical Studies

Decapeptide-12 and Melasma

One clinical study aimed to evaluate the potential of Decapeptide-12 in test subjects with moderate to severe melasma, solar lentigines, periocular lines, and wrinkles.⁽¹⁾ This 24-week experiment reported apparent improvements in all of the reported facial conditions among the 25 subjects, with sustained impact.

Another clinical trial investigated the potential of Decapeptide-12 on mild-to-moderate melasma in 33 test subjects over 16 weeks.⁽²⁾ Results suggested a visible reduction in the appearance of melasma.

Furthermore, one study reported a complete clearance of melasma in 25% of subjects after six weeks of Decapeptide-12 presentation.⁽³⁾ Decapeptide-12 also was reported by the researchers to exhibit an apparent impact in test subjects with the Fitzpatrick phototype IV skin type and moderate recalcitrant melasma completed.⁽⁴⁾ Subjects with Fitzpatrick skin type IV are reportedly some of the most common melasma sufferers. The researchers concluded that: “All […] demonstrated statistically significant improvement in the appearance of melasma and overall facial aesthetics.”

Decapeptide-12 and Post-inflammatory Hyperpigmentation

A clinical case study on pigmented skin (Fitzpatrick skin type IV) indicated that Decapeptide-12 may possibly accelerate the clearance of post-inflammatory hyperpigmentation compared to placebo.⁽⁵⁾ The researchers suggest this might be due to the tyrosinase-inhibiting potential of Decapeptide-12.⁽⁶⁾

Decapeptide-12 and Solar Lentigo

One study evaluated the impact of Decapeptide-12 in the form of hyperpigmentation called solar lentigines caused by chronic photodamage.⁽⁷⁾ The results reported that 38.5% of the models evaluated appeared to have achieved complete clearance, and all subjects appeared to exhibit some improvement. Furthermore, 30.7% of the models were reported to improve from a moderate degree of photodamage to a milder degree, 15.4% improved from a severe degree to a moderate degree, and another 15.4% improved from a severe degree to a milder degree after 24 weeks.

Decapeptide-12 and Cell Aging

Sirtuins are a family of genes involved in various cellular processes. They are believed to regulate cellular metabolism, DNA repair, inflammation, and stress resistance. One of the most well-known sirtuins is SIRT1, which has been suggested to regulate various biological pathways, such as glucose metabolism, lipid metabolism, and cellular stress responses. Studies have also suggested that SIRT1 may be involved in extending the lifespan in certain model organisms. One of the most promising compounds is resveratrol, found in red wine, and has been suggested to activate SIRT1 in some studies.

One study looked at the potential of Decapeptide-12 on sirtuin gene expression levels in keratinocyte progenitors.⁽⁸⁾ The researchers used RT-PCR to measure the impact of Decapeptide-12 on seven Sirtuin genes and cellular viability and proliferation after 72-hour incubation with various concentrations of Decapeptide-12. The results suggested that Decapeptide-12 possibly increased the transcription of several Sirtuin genes, including SIRT1, SIRT3, SIRT6, and SIRT7, with reportedly reduced cytotoxicity. The researchers reported that “ decapeptide-12 increased transcription of SIRT1 by 141 ± 11% relative to control cells, whereas levels of SIRT3, SIRT6, and SIRT7 were increased by 121 ± 13%, 147 ± 8% and 95± 14%, respectively.”

SIRT1, with a reported increase in transcription by 141 ± 11% may enhance cellular resilience against oxidative stress and inflammation, possibly delaying aging processes on a cellular level. The apparent increases in SIRT3 (121 ± 13%) and SIRT6 (147 ± 8%) transcription levels further amplify the possible research outcomes. SIRT3’s potential involvement in mitochondrial function and energy metabolism suggests that decapeptide-12 might enhance mitochondrial efficiency and antioxidant capacity. Similarly, SIRT6 is possibly associated with DNA repair, telomere maintenance, and inflammation regulation. Its potential upregulation might contribute to improved genomic stability and reduced inflammation, potentially further decelerating the aging process in cells. While the reported increase in SIRT7 transcription (95 ± 14%) appears less pronounced, it may still indicate potential influence on nucleolar functions, including ribosome biogenesis and stress sensing. This subtle modulation might also contribute to the overall cellular homeostasis and longevity.⁽⁸⁾

Decapeptide-12 is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.

References:

1. Jiang, L., Hino, P. D., Bhatia, A., Stephens, T. J., & Jimenez, F. (2018). Efficacy of Trifecting® Night Cream, a Novel Triple acting Skin Brightening Product: A Double-blind, Placebo-controlled Clinical Study. The Journal of clinical and aesthetic dermatology, 11(12), 21–25.
2. Ramírez, S. P., Carvajal, A. C., Salazar, J. C., Arroyave, G., Flórez, A. M., & Echeverry, H. F. (2013). Open-label evaluation of a novel skin brightening system containing 0.01% decapeptide-12 in combination with 20% buffered glycolic acid for the treatment of mild to moderate facial melasma. Journal of drugs in dermatology : JDD, 12(6), e106–e110.
3. Hantash, B. M., & Jimenez, F. (2012). Treatment of mild to moderate facial melasma with the Lumixyl brightening system. Journal of drugs in dermatology : JDD, 11(5), 660–662.
4. Hantash, B. M., & Jimenez, F. (2009). A split-face, double-blind, randomized and placebo-controlled pilot evaluation of a novel oligopeptide for the treatment of recalcitrant melasma. Journal of drugs in dermatology : JDD, 8(8), 732–735.
5. Bhatia, A., Hsu, J. T.s, & Hantash, B. M. (2014). Combined delivery and dermalinfusion of decapeptide-12 accelerates resolution of post-inflammatory hyperpigmentation in skin of color. Journal of drugs in dermatology : JDD, 13(1), 84–85.
6. Chen, J., Bian, J., Hantash, B. M., Albakr, L., Hibbs, D. E., Xiang, X., Xie, P., Wu, C., & Kang, L. (2021). Enhanced skin retention and permeation of a novel peptide via structural modification, chemical enhancement, and microneedles. International journal of pharmaceutics, 606, 120868. https://doi.org/10.1016/j.ijpharm.2021.120868
7. Kassim, A. T., Hussain, M., & Goldberg, D. J. (2012). Open-label evaluation of the skin-brightening efficacy of a skin-brightening system using decapeptide-12. Journal of cosmetic and laser therapy : official publication of the European Society for Laser Dermatology, 14(2), 117–121. https://doi.org/10.3109/14764172.2012.672745
8. Basil, M. H., & Anan, A. U. (2019). Tyrosinase inhibitors with potent anti-senescence activity in human neonatal keratinocyte progenitors. J Dermatol Surg Res Ther, 2019, 30-39.

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Pentapeptide-18 (Leuphasyl)

Pentapeptide-18 is a synthetic peptide composed of five amino acids (H-Tyr-Ala-Gly-Phe-Leu-OH) that were developed to mimic the natural process of suppressing muscle contractions, consequently reducing the development and depth of wrinkling along the epidermal barrier. Pentapeptide-18 has been hypothesized by researchers to interact with the neuroreceptors in the skin, potentially inhibiting the release of acetylcholine, a neurotransmitter that triggers muscle contractions.⁽¹⁾

Pentapeptide-18 has also been suggested to impact skin cell function. It may potentially help to increase skin barrier elasticity through the stimulation of key proteins collagen and elastin. Both these proteins are considered to be a crucial component of the skin’s extracellular matrix, and their production tends to decrease over time.

Chemical Makeup⁽²⁾

Molecular Formula: C₂₉H₃₉N₅O₇
Molecular Weight: 569.65 g/mol
Other Known titles H-Tyr-Ala-Gly-Phe-Leu-OH, Leuphasyl

Research and Clinical Studies

Pentapeptide-18 and Wrinkling, Skin Structure

A 2014 study investigated the potential of Pentapeptide-18 (Leuphasyl) in reducing the depth and length of wrinkles and creases along the stratum corneum of the skin. This study evaluated the impact on moderate to severe wrinkles exposed to a Pentapeptide-18 formulation twice a day for 28 days. Digital imaging and silicone replicas were used to determine an apparent reduction in the depth of the wrinkles, with an average reduction of 11.31%. As per Anca O. Dragomirescu et al., “Leuphasyl is an active synthesis peptide… The efficiency of this molecule is evidently inferior to botulinum toxin … but it [may be] free from side effects and it confers an aspect of wrinkles’ attenuation.” ⁽¹⁾

Research indicates that Pentapeptide-18 may be highly specific. Clinical studies have suggested a statistically significant reduction of 2% to 9% in the appearance of wrinkles. In a randomized, double-blind, placebo-controlled study, researchers evaluated the depth of wrinkles and skin smoothness following peptide exposure using various methods such as skin imaging, dermatological assessments, and subjective self-assessments. The results suggested an overall reduction in the depth of wrinkles and increased skin smoothness after four weeks.⁽³⁾

Pentapeptide-18 and Fine Lines

Scientists posit that Pentapeptide-18 may reduce fine lines, due to its potential ability to decrease glutamate release by 11%. This potential was apparently noticed following two months of experimentation in one study. This reduction suggests that Pentapeptide-18 might influence neurotransmitter pathways, possibly involved in the control of muscle contractions beneath the skin. The modulation of glutamate, a key excitatory neurotransmitter, might hypothetically lead to decreased muscular activity, thereby reducing the formation and depth of fine lines.⁽⁴⁾

In addition to reducing glutamate, Pentapeptide-18 may also suppress acetylcholine. The potential mechanism suggested involves decreased acetylcholine secretion within the synaptic cleft. This hypothesis is grounded on observing enkephalins’ typical function in modulating neurotransmitter release. Enkephalins, which are part of the endogenous opioid peptides, are believed to potentially inhibit neurotransmitter release, and this property is thought to possibly extend to the action of Pentapeptide-18. Specifically, the interaction between Pentapeptide-18 and neural receptors might lead to an inhibition of acetylcholine release. This inhibition may be mediated through the modulation of calcium influx into presynaptic neurons. Calcium plays a crucial role in the exocytosis of neurotransmitters, and its reduction within neurons is often linked to decreased neurotransmitter secretion. Therefore, it is conceivable that Pentapeptide-18 may contribute to this pathway, possibly by mimicking the regulatory actions of enkephalins on calcium channels.⁽⁵⁾

Pentapeptide-18 and Melanogenesis

Park et al. (2020) explored the potential actions of D-tyrosine-containing cosmetic Pentapeptide-18 derivatives on melanogenesis.⁽⁶⁾ The modifications to these peptides involved substituting the N-terminal L-tyrosine with D-tyrosine or appending L/D-tyrosine at the C-terminus. This research utilized melanoma MNT-1 cells to evaluate these possibilities. The findings tentatively suggest that alterations in the peptide structure may potentially affect melanogenesis. It is hypothesized that the presence of D-tyrosine, particularly when located at the C-terminal end of the peptide chain, might contribute to a reduction in melanogenesis. This observation was notable in Pentapeptide-18 analogs featuring C-terminal D-tyrosine. The results seem to indicate that the positioning and orientation of the tyrosine residues within the peptide might play a significant role. D-tyrosine, the enantiomer of the naturally occurring L-tyrosine, might conceivably modify the peptide’s interactions with enzymes or receptors involved in melanin synthesis, potentially leading to decreased melanin production in the cells.

Pentapeptide-18 peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.

References

1. Dragomirescu, A. O., Andoni, M., Ionescu, D. & Andrei, F. The Efficiency and Safety of Leuphasyl—A Botox-Like Peptide. Cosmetics 1, 75–81 (2014). https://www.mdpi.com/2079-9284/1/2/75
2. Leucine,L-tyrosyl-L-alanylglycyl-L-phenylalanyl National Center for Biotechnology Information (2023). PubChem Compound Summary for CID 44568, Pentapeptide-18.
3. Puig, A., Garcia-Anton, J., Perez, R. & Mangues, M. Eyeseryl and Leuphasyl: Synthetic Peptides as Advanced Cosmetic Actives. Available at http://www.cosmeticsciencetechnology.com/companies/articles/821.pdf.
4. Schagen SK. Peptide Treatments with Effective Anti-Aging Results. Cosmetics. 2017; 4(2):16. https://doi.org/10.3390/cosmetics4020016
5. Errante F, Ledwoń P, Latajka R, Rovero P, Papini AM. Cosmeceutical Peptides in the Framework of Sustainable Wellness Economy. Front Chem. 2020 Oct 30;8:572923. doi: 10.3389/fchem.2020.572923. PMID: 33195061; PMCID: PMC7662462.
6. Park J, Jung H, Jang B, Song HK, Han IO, Oh ES. D-tyrosine adds an anti-melanogenic effect to cosmetic peptides. Sci Rep. 2020 Jan 14;10(1):262. doi: 10.1038/s41598-019-57159-3. PMID: 31937863; PMCID: PMC6959337.

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Syn-AKE

Syn-AKE is a synthetic peptide with the sequence beta-alanyl-L-prolyl-3-aminomethyl-L-alanine benzyl amide acetic acid known as tripeptide-3. The structure of Syn-AKE is composed of the amino acids alanine, proline, and diamino butyrate, which are linked by peptide bonds.⁽¹⁾ The peptide is designed to mimic the activity of Waglerin-1, a polypeptide. Waglerin-1 is a muscle relaxant that is considered to block the action of acetylcholine in the neuromuscular junction, leading to a decrease in muscle contractions.

When developing Syn-AKE, researchers aimed to develop a peptide with similar activity on muscle contractions as Waglerin-1. The peptide’s intended mechanism of action is temporarily inhibiting muscle contractions, which typically leads to a decrease in the depth of wrinkles on the skin of test subjects. This compound has been extensively researched for its potential anti-aging properties for the skin of various species, including reducing fine lines and wrinkles, improving skin texture, and increasing skin hydration solely because of its muscle-relaxing properties.

Chemical Makeup

Molecular formula: C₂₃H₃₇N₅O₇
Molecular weight: 495.57 g/mol
Other known titles: Tripeptide-3, Syn-Ake acetate, SYN-AK, DTXSID40231699, EX-A3743

Research and Clinical Studies

Syn-AKE Peptide Mechanism of Action

Syn-AKE has been reported by researchers to mimic the action of Waglerin-1.⁽²⁾ Waglerin-1 has been considered to have muscle-relaxant properties. According to researchers, this component is a 22-amino acid polypeptide, and may be potentially selective for the form of nicotinic acetylcholine receptors (nAChRs).⁽³⁾ The nACh receptors transmit signals from nerve cells to muscle cells, ultimately leading to muscle contractions. By blocking the activity of nAChRs, Waglerin-1 apparently prevents the release of acetylcholine and blocks muscle contraction. Waglerin-1 is also suggested to have modulating impacts on the brain’s neurotransmitter gamma-aminobutyric acid (GABA) receptors. These receptors are involved in regulating the activity of neurons and by modulating them, Waglerin-1 may cause significant risks in research settings.

Contrastingly, initial research suggests Syn-AKE cannot affect GABA receptors in the brain and may lack the risks of Waglerin-1. Syn-AKE was designed to mimic the activity of Waglerin-1 by targeting the same nAChRs in the neuromuscular junctions. Specifically, Syn-AKE is a tripeptide that contains a sequence of amino acids similar to the region of Waglerin-1 that binds to nAChRs.

Syn-AKE is thought to have great permeability through the skin and bind to the nAChRs in the muscles beneath it, possibly preventing them from responding to acetylcholine. Researchers suggest that the peptide may be particularly impactful against expression lines by relaxing facial muscles. According to experimental research, the peptide “was able to reduce the frequency of innervated muscle cell contractions by 82% (…) after 2h of [presentation].“⁽⁴⁾

The antagonism of Syn-AKE towards the nAChRs may be reversible.⁽⁵⁾⁽⁶⁾ Such a reversal may indicates that the potential of tripeptide-3 on the receptors are temporary and can be reversed once the peptide is no longer present.

Syn-AKE Peptide and Fine Lines, Wrinkles

According to researchers, Syn-AKE may induce an immediate minimization of muscle contraction, reducing fine lines and wrinkles.⁽⁷⁾⁽⁸⁾ A three-month study including 37 female subjects aged 33 to 45 with mild-to-moderate wrinkles reported that Syn-AKE appeared to exhibit both immediate and long-term potential.⁽⁹⁾ Assessments indicated statistically significant improvements in wrinkles shortly after presentation and at months 1 and 3.

One of the largest studies conducted on Syn-AKE compared its potential with other peptides and a placebo in 45 test subjects. Syn-AKE was reported to exhibit some potential, gradually exhibiting greater action after repeated presentation and reaching more than 50% after four weeks. Researchers suggested that Syn-AKE “showed up to a 52% reduction in the appearance of wrinkle size in test volunteers after a 28-day application of a 4% formulation to the forehead twice a day“^(10)(11)

Syn-AKE peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.

References:

1. Balaev, A. N., Okhmanovich, K. A., & Osipov, V. N. (2014). A shortened, protecting group free, synthesis of the anti-wrinkle venom analogue Syn-Ake exploiting an optimized Hofmann-type rearrangement. Tetrahedron Letters, 55(42), 5745-5747.
2. Molles, B. E., Tsigelny, I., Nguyen, P. D., Gao, S. X., Sine, S. M., & Taylor, P. (2002). Residues in the epsilon subunit of the nicotinic acetylcholine receptor interact to confer selectivity of waglerin-1 for the alpha-epsilon subunit interface site. Biochemistry, 41(25), 7895–7906. https://doi.org/10.1021/bi025732d
3. Gorouhi, F., & Maibach, H. I. (2009). Role of peptides in preventing or treating aged skin. International journal of cosmetic science, 31(5), 327–345. https://doi.org/10.1111/j.1468-2494.2009.00490.x
4. Reddy, B., Jow, T., & Hantash, B. M. (2012). Bioactive oligopeptides in dermatology: Part I. Experimental dermatology, 21(8), 563–568. https://doi.org/10.1111/j.1600-0625.2012.01528.x
5. Munawar, A., Ali, S. A., Akrem, A., & Betzel, C. (2018). Snake venom peptides: Tools of biodiscovery. Toxins, 10(11), 474.
6. TATARINGA, G., & ZBANCIOC, A. M. (2021). Antirid peptides in cosmeceutical formula. Romanian Journal of PHARMACEUTICAL PRACTICE| Vol. XIV, 58(3).
7. Chhipa, N. M., & Chaudhari, B. (2012). Toxin as a Medicine. Journal of Current Pharmaceutical Research, 9(1), 11-8.
8. Trookman, N. S., Rizer, R. L., Ford, R., Ho, E., & Gotz, V. (2009). Immediate and Long-term Clinical Benefits of a Treatment for Facial Lines and Wrinkles. The Journal of clinical and aesthetic dermatology, 2(3), 38–43.
9. Reddy, B. Y., Jow, T., & Hantash, B. M. (2012). Bioactive oligopeptides in dermatology: Part II. Experimental dermatology, 21(8), 569–575. https://doi.org/10.1111/j.1600-0625.2012.01527.x
10. Pai, V. V., Bhandari, P., & Shukla, P. (2017). Peptides as cosmeceuticals. Indian Journal of Dermatology, Venereology and Leprology, 83, 9.

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