The interest in identifying active chemicals to safeguard skin health has been intesifying over the past decade. Studies suggest that with their range of biological potential including antioxidation, anti-aging, antidiabetes, antihypertension, and antibacterial properties, bioactive peptides may be promising compounds for the study of aging skin. Recent years have seen substantial in vitro and experimental studies of natural and synthesized anti-aging peptides.
Research suggests collagen and other anti-aging peptides may significantly protect skin from environmental damage. This data suggests that bioactive peptides may have the potential to enhance skin health by performing a variety of useful physiological activities. In this article, we compiled the findings from studies on anti-aging peptides and their use in finishing products to enhance skin health, focusing on collagen peptides and related synthetic peptides.
Collagen Peptides
Collagen is a widespread protein. Collagen types I, II, III, IV, and others are often identified in research studies. Collagen a structural protein that is considered to support cellular connection, resulting in such impacts asincreasing strength and firmness of tissues. Moreover, collagen protein may reinforce and maintain cell structures in tissues, including tendons, skin, and teeth. Previous research has suggested that enzymatic hydrolysis of collagen may produce bioactive peptides with various physiological potential. Hydrolyzed collagen and peptides produced from collagen have been speculated to aid the skin.
When collagen is heated, it changes into a gelatin that is soluble in water. Investigations imply that collagen peptides may be synthetically developed using gelatin and an enzymatic process. As Pyun H-B et al. proposed, collagen peptides may have several biological roles, including antioxidation, cell proliferation, and chemotaxis. For instance, it may recover collagen degradation and elastic fiber abnormalities caused by ultraviolet radiation by inhibiting dermal collagen decomposition by reducing collagenase (matrix metalloproteinases: MMP-3 and MMP-13) and gelatinase activity (MMP-2 and MMP-9).
Kang et al. utilized collagen peptides on hairless mice to UV light for 9 weeks. Collagen peptides were speculated to up-regulate the expression of hyaluronidase (HYAL-1 and HYAL-2) mRNA while simultaneously increasing the expression of hyaluronic acid synthase mRNA and skin moisturizing factor filaggrin.
Palmitoyl- Peptide
Studies suggest that peptide stability and permeability may be greatly enhanced by combining them with fatty acids Palmitate, the most common fatty acid, may link two protein molecules by covalent alteration. As suggested by research by Foldvari et al., the lipophilicity of palmitate residues in palmitoyl-derived -interferon may increase the penetration of natural protein into the skin by a factor of five. Additionally, several studies have suggested that Palmitoyl binding polypeptide may enhance the polypeptide’s skin penetration. It has been hypothesized that it is possible to boost the penetration rate by a factor of 100–1000 compared to that of a regular polypeptide.
Acetyl- Peptide
Proteins are often acetylated by an acetyl-converting enzyme, which transfers the acetyl group from an acetyl donor such as acetyl-CoA to a target lysine residue. Also, the N-terminus of synthetic peptides is where acetylation often happens.
These tetrapeptides have been speculated to encourage the growth of keratinocytes and stimulate the synthesis of type I collagen protein and basement membrane glycan. An experimental study has proposed that Tetrapeptide-9 and Tetrapeptide-11 may increase skin thickness and firmness. In addition, these peptides may have a 5-10% greater impact on the skin than a placebo.
Researchers Wang Y et al. proposed a similar pattern when they randomly assigned 60 research models to receive either Argireline (Glu-Glu-Met-Gln-Argacetyl hexapeptide) or a placebo. Argireline appeared to have inhibited vesicle docking and wrinkle formation by blocking catecholamine release, resulting in an impact rate of up to 48.9%. Also, the Ser-Asp-Lys-Pro acetyl tetrapeptide was hypothesized to enhance skin regeneration and hair development and potentially mitigate age-associated skin degradation or alopecia.
Copper Tripeptides/ Manganese
Copper peptide, a short peptide chelated with Cu2+ and exhibiting high impact, has a molecular weight of 700 Daltons (da). Picart et al. isolated a copper tripeptide (Cu-GHK) with the sequence Gly-His-Lys. They speculated that this peptide may be used as the active substance in the synthesis of albumin, allowing the liver tissue synthesizer of mature research models to function at a level comparable to that of younger models.
Among copper peptides, the Cu-GHK complex is now one of the most researched peptidesdue to its potential properties of stimulating wound healing and skin regeneration and lowering wrinkle depth, skin laxity, and skin discoloration. Studies suggest that collagen, elastin, and glycosaminoglycan production may be boosted, leading to visibly better skin.
Leyden et al. and Finkley et al. proposed that Cu-GHK may influence skin elasticity, humidity, and wrinkles. Manganese (Mn) is a trace element considered essential for wound healing. Peptides, interestingly, may be put to work carrying trace elements. After 12 weeks of use in a serum formulation, manganese tripeptide (GHK-Mn2+) appeared to be effective in managing mild damage to facial skin.
Researchers interested in further studying these compounds may find collagen peptides for sale on Core Peptides website, the online highest-quality peptide source.
References
[i] Kim, D.-U., Chung, H.-C., Choi, J., Sakai, Y., & Lee, B.-Y. (2018). Oral intake of lowmolecular-weight collagen peptide improves hydration, elasticity, and wrinkling in human skin: A randomized, double-blind, placebo-controlled study. Nutrients, 10(7), 826. https://doi.org/10.3390/nu10070826.
[ii] Pyun, H.-B., Kim, M., Park, J., Sakai, Y., Numata, N., Shin, J.-Y., Shin, H.-J., Kim, D.-U., & Hwang, J.-K. (2012). Effects of collagen tripeptide supplement on photoaging and epidermal skin barrier in UVB-exposed hairless mice. Preventive Nutrition and Food Science, 17(4), 245–253. https://doi.org/10.3746/pnf.2012.17.4.245.
[iii] Kang, M. C., Yumnam, S., & Kim, S. Y. (2018). Oral intake of collagen peptide attenuates ultraviolet B irradiation-induced skin dehydration in vivo by regulating hyaluronic acid synthesis. International Journal of Molecular Science, 19(11), 3551. https://doi.org/10.3390/ijms19113551
[iv] Benson, H. A., & Namjoshi, S. (2008). Proteins and peptides: Strategies for delivery to and across the skin. Journal of Pharmaceutical Science, 97(9), 3591–3610. https://doi.org/10.1002/jps.21277
[v] Foldvari, M., Attah-Poku, S., Hu, J., Li, Q., Hughes, H., Lorne, A. B., & Kruger, S. (1998). Palmitoyl derivatives of interferon α: Potential for cutaneous delivery. Journal of Pharmaceutical Science., 87(10), 1203–1208. https://doi.org/10.1021/js980146k.
[vi] Dominik, I., Eileen, J., Marc, H., Remo, C., Eliane, W., & Hugo, Z. (2015). Activation of
TGF-β: A gateway to skin rejuvenation. Peptides, 10(6), 6–11.
[vii] Allfrey, V., Faulkner, R., & Mirsky, A. (1964). Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proceedings of the National Academy of Sciences of the United States of America, 51(5), 786–794. https://doi.org/10.1073/pnas.51.5.786.
[viii] Schagen, S. K. (2017). Topical peptide treatments with effective anti-aging results. Cosmetics, 4(2), 16. https://doi.org/10.3390/cosmetics4020016.
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