Among many naturally occurring proteins, collagen is considered to be plentiful and distributed extensively. Types I, II, III, and IV collagen, among others, are often studied. Tissue strength and structural integrity are two examples of the kinds of organizational structures that this protein  is considered to help to maintain. The protein collagen strengthens and stabilizes cell structures in tissues and may also support connective tissues, including tendons, skin, and teeth and fangs. Past research has indicated that the enzymatic hydrolysis of collagen may result in the release of bioactive peptides that may serve several physiological purposes. Studies suggest the skin’s condition may be improved with these collagen hydrolysates and peptides generated from collagen.

Collagen Peptides: Mechanism of Action

When heated, collagen may transform into gelatin that dissolves in water. In addition, gelatin can enzymatically create collagen peptides. Antioxidation, cell proliferation, and chemotaxis were among the several biological roles Pyun H-B et al. suggested for collagen peptides. To give just one example, it has been hypothesized to prevent the breakdown of dermal collagen by decreasing the activity of matrix metalloproteinases like MMP-3 and MMP-13 as well as gelatinase, which in turn might reduce skin cell moisture loss and wrinkles, control skin hydration, increase skin elasticity, and restore collagen degradation and abnormalities in elastic fibers caused by UV radiation.

A group of hairless mice were subjected to UV radiation by researchers, and for nine weeks, some of the animals were given collagen peptides. As speculated by the scientists, collagen peptides may upregulate the expression of hyaluronidase (HYAL-1 and HYAL-2) mRNA, raise the quantity of hyaluronic acid in skin tissue, and upregulate the expression of skin moisturizing factor filaggrin and hyaluronic acid synthase mRNA. That is to say, according to specialists, collagen peptide consumption may help prevent UVB-induced skin moisture loss.

Collagen Peptides and Skin

Findings imply that regarding anti-cell aging impacts within the skin cells, various collagen peptide sources might work differently. Researchers asserted that taking collagen peptide from pig collagen I for 4-8 weeks may stimulate the production of skin proteins such as fibrin, elastin, and procollagen I.

According to research by Offengenden et al., which examined the effects of chicken-derived collagen peptides on skin fibroblasts, this peptide may significantly affect inflammatory alterations, oxidative stress, collagen I production, and cell proliferation. In addition, studies suggest that when presented, collagen peptides from bovine bone may increase collagen content and alter the ratio of type I to type III collagen, contributing to skin relaxation. However, they did not find any significant impact on skin moisturizing.

Research suggests that another method developed and utilized to address skin issues is possibly the extraction of collagen peptides from aquatic animals. Scientists have previously isolated a collagen peptide from hydrolyzed tilapia collagen with the sequence YGDEY (Tyr-Gly-Asp-Glu-Tyr). Researchers indicated that it may have many properties, including increasing the expression of antioxidant factors like glutathione and superoxide dismutase (GSH), keeping reduced and oxidized glutathione levels balanced, improving type I procollagen generation, significantly reducing ROS levels in keratinocytes (HaCaT), preventing DNA oxidative damage, inhibiting the expression of collagenase and gelatinase, and more.

Furthermore, it was speculated that the Ala-Tyr dipeptide, derived from carp skin hydrolysate, may have high antioxidant activity and might be used in this capacity. The properties of dipeptide over other antioxidant peptides are hypothesized to be its small molecular weight, ease of absorption, and practical use. Regarding skin cell aging resistance, dipeptide has been speculated to offer certain properties. Therefore, further comprehensive studies and developments are required.

Research suggests the anti-cell aging potential of collagen hydrolysate and collagen peptide on the skin is attributed, in part, to the hydroxyproline-containing peptide’s remarkable stability in the face of enzyme activity after the hydrolysate is presented. Scientists hypothesize that because of this, the collagen peptide may be used for anti-aging purposes on the skin more effectively and with more stability even after it has been digested in the intestines. Collagen peptides consumed from diverse sources may cause differences in plasma and skin levels and types, as research suggests.

Investigations purport that the Pro-Hyp and Hyp-Gly collagen sequences may be more significant than other collagen peptides due to their biological action on the skin. It has been theorized that Pro-Hyp might boost the generation of hyaluronic acid by skin fibroblasts and stimulate the proliferation of mouse skin fibroblasts on collagen. As research suggests, hyp-Gly may also promote the expansion of skin fibroblasts in mice. It was ascertained to have a greater impact on fibroblast collagen gel growth promotion than Pro-Hyp. Gly-Pro dipeptide, a characteristic low molecular weight peptide in fish scale collagen hydrolysate, was indicated to be helpful to skin cell function in a study by Lee et al., who synthesized and examined fish scale collagen peptide and its physiological function.

If you are a researcher interested in further studying the potential of these compounds on the skin, buy collagen peptides from Biotech Peptides.

References

[i] D. Schuppan et al. Collagens in the liver extracellular matrix bind hepatocyte growth factor

Gastroenterology (1998)

[ii] R. Mayne et al. New members of the collagen superfamily Curr. Opin. Cell Biol. (1993)

[iii] H. Hofmann et al. The role of polar and hydrophobic interactions for the molecular packing of type I collagen: a three-dimensional evaluation of the amino acid sequence J. Mol. Biol. (1978)

[iv] T.M. Schmid et al. Immunoelectron microscopy of type X collagen: supramolecular forms within embryonic chick cartilage.

[v] B.G. Hudson et al. Type IV collagen: structure, gene organization, and role in human diseases. Molecular basis of Goodpasture and Alport syndromes and diffuse leiomyomatosis