Identification of chia seed (Salvia hispanica L.) peptides with enzyme inhibition activity towards skin-aging enzymes.

Chia (Salvia hispanica) seed peptides have drawn attention because of their antioxidant, antihypertensive and anti-inflammatory activities, making them ideal candidates for development of cosmeceutical skin products. However, there are no preceding reports that address their aging-related enzyme inhibitory activities. The aim of this study was to investigate the in vitro and in silico inhibitory activity of chia seed peptides towards the main aging-related enzymes. Enzyme-inhibition activity of < 3 kDa chia seed peptides towards collagenase, hyaluronidase, tyrosinase, and elastase was evaluated. Further fractions were obtained by size exclusion chromatography (SEC) and re-tested for enzyme inhibitory activity. Peptide sequences were identified from the most effective fraction and used for in silico analysis. The < 3 kDa peptides exhibited inhibitory activities towards elastase (65.32%, IC50 = 0.43 mg/mL), tyrosinase (58.74%, IC50 = 0.66 mg/mL), hyaluronidase (26.96%, IC50 = 1.28 mg/mL), and collagenase (28.90%, IC50 = 1.41 mg/mL). They showed mixed-type inhibition patterns towards elastase and hyaluronidase, while a non-competitive inhibition pattern was observed towards collagenase and tyrosinase. Fraction II obtained by SEC, showed higher enzyme inhibitory activity. Seven peptides were identified in this fraction (APHWYTN, DQNPRSF, GDAHWAY, GDAHWTY, GDAHWVY, GFEWITF, and KKLKRVYV), which according to in silico analysis, possess 19-29 enzyme-peptide pair interactions towards elastase and three peptide sequences shared homology sequence (GDAHW). These results demonstrate that peptides from chia seeds may contribute in the improvement of skin health by offering protection against aging-related enzymes by preventing degradation of the protein matrix on the skin; however, further in vivo studies are needed to evaluate its actual capability.