Chicken collagen hydrolysates differentially mediate anti-inflammatory activity and type I collagen synthesis on human dermal fibroblasts

Collagen is a major extracellular matrix protein. Given the potential anti-inflammatory and antioxidant profiles of these bioactive compounds, there has been increasing interest in using collagen derived peptides and peptide-rich collagen hydrolysates for skin health, due to their immunomodulatory, antioxidant and proliferative effects on dermal fibroblasts. However, all hydrolysates are not equally effective in exerting the beneficial effects; hence, further research is needed to determine the factors that improve the therapeutic applicability of such preparations. We used different enzymatic conditions to generate a number of different collagen hydrolysates with distinct peptide profiles. We found that the use of two rather than one enzyme for hydrolysis generates a greater abundance of low molecular weight peptides with consequent improvement in bioactive properties. Testing these hydrolysates on human dermal fibroblasts showed distinct actions on inflammatory changes, oxidative stress, type I collagen synthesis and cellular proliferation. Our findings suggest that different enzymatic conditions affect the peptide profile of hydrolysates and differentially regulate their biological activities and potential protective responses on dermal fibroblasts.