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Characterization of a Collagenase-1 Inhibitory Peptide Purified from Skate Dipturus chilensis Skin

홍어류(Dipturus chilensis) 껍질로부터 분리 정제된 collagenase-1 저해 펩타이드의 특성

  • Park, Sung-Ha (Department of Marine Biotechnology, Gangneung-Wonju National University) ;
  • Lee, Jung-Kwon (Department of Marine Biotechnology, Gangneung-Wonju National University) ;
  • Jeon, Joong-Kyun (Department of Marine Biotechnology, Gangneung-Wonju National University) ;
  • Byun, Hee-Guk (Department of Marine Biotechnology, Gangneung-Wonju National University)
  • 박성하 (강릉원주대학교 해양생물공학과) ;
  • 이정권 (강릉원주대학교 해양생물공학과) ;
  • 전중균 (강릉원주대학교 해양생물공학과) ;
  • 변희국 (강릉원주대학교 해양생물공학과)
  • Received : 2011.06.08
  • Accepted : 2011.10.07
  • Published : 2011.10.31

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, ${\alpha}$-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 $IC_{50}$ value of purified peptide was 87.0 ${\mu}M$. Moreover, the peptide did not exhibit cytotoxic effects on human dermal fibroblast cell lines.

Keywords

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