광어껍질 펩신 가수분해물 유래 콜라게네이즈 저해 펩타이드의 서열분석과 분자도킹

Abstract

Bioactive peptides were isolated from the peptic hydrolysate of flounder skin using chromatographic methods, and their amino acid sequence was identified. The collagenase inhibitory ability of the hydrolysate was evaluated. Seven peptides, including Gln-Phe, Val-Ile-Cys-Glu, Arg-Gly-Glu, Val-Asp-Leu, Gly-Pro-Met, Gly-Ser-Ala-Pro-Glu, and Arg-Leu, were identified using matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF) mass spectrometry. Six peptides in the range of 6 to 18 amino acid residues were identified using LC/quadrupole time-of-flight (Q-TOF) mass spectrometry. All the peptides were verified on the type I collagen α-1 chain obtained from the Bastard halibut of Unitprot (www.uniprot.org) (code number: Q5NT96). Analysis of the seven peptides from the MALDI-TOF mass spectrometry was carried out using in silico simulation tools, and four peptides were further assessed for their potential collagenase inhibitory activities. The amino acid sequence of Val-Ile-Cys-Glu showed the highest GOLD score of 83.9 in in silico molecular docking and inhibited the collagenase activity up to 83% compared to control. Gly-Pro-Hyp, a quality index for the product, was also verified by the high-performance liquid chromatography (HPLC) method and measured 156 μg/g in the hydrolysate. These results suggest that the peptic hydrolysate from flounder skin contains small peptides with high collagenase inhibitory activity. This hydrolysate may find application as a food material or as an ingredient in skin products with an anti-wrinkle function. ? 2022 The Korean Society of Food Science and Nutrition. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (https://creativecommons.org/lice nses/by-nc/4.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.