Abstract
We attempted to isolate a collagenase-1 inhibitory peptide from skate Dipturus chilensis skin protein. The protein from skate skin was digested by various enzymes (alcalase, <TEX>${\alpha}$</TEX>-chymotrypsin, neutrase, papain, pepsin, and trypsin) to produce a collagenase-1 inhibitory peptide. The collagenase-1 inhibitory activity of the peptides obtained was measured by gelatin digestion assay. Among the six hydrolysates, pepsin hydrolysate exhibited the highest collagenase-1 inhibitory activity. The peptide showing strong collagenase-1 inhibitory activity was purified by Sephadex G-25 gel chromatography and HPLC using an octadecylsilyls (ODS) column. The amino acid sequence of purified collagenase-1 inhibitory peptide was identified to be Asn-Leu-Asp-Val -Leu-Glu-Val-Phe (961 Da) by quadrupole time of flight (Q-TOF) and electrospray ionization mass spectrometry (ESI-MS) mass spectroscopy. The <TEX>$IC_{50}$</TEX> value of purified peptide was 87.0 <TEX>${\mu}M$</TEX>. Moreover, the peptide did not exhibit cytotoxic effects on human dermal fibroblast cell lines.
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