文献类型：期刊文献

中文题名：Inhibitory effect of a Chinese quince seed peptide on protein glycation:A mechanism study

作者：Yejun Deng[1] Xiang Wang[1] Caihong Zhang[1] Pujun Xie[1] Lixin Huang[1,2]

第一作者：邓叶俊

机构：[1]National Engineering Laboratory for Biomass Chemical Utilization,Key and Open Laboratory of Forest Chemical Engineering,National Forestry and Grassland Administration,Key Laboratory of Biomass Energy and Material,Institute of Chemical Industry of Forest Products,Chinese Academy of Forestry,Nanjing,Jiangsu 210042,China;[2]Co-Innovation Center of Efficient Processing and Utilization of Forest Resources,Nanjing Forestry University,Nanjing 210037,China

年份：2023

卷号：8

期号：2

起止页码：187-197

中文期刊名：生物质资源与工程(英文)

外文期刊名：Journal of Bioresources and Bioproducts

收录：Scopus;CSCD:【CSCD2023_2024】；

基金：support for this work by National Natural Science Foundation of China (No.32171732).

语种：英文

中文关键词：Peptide;Chinese quince seed;Antiglycation;Molecular docking simulation

分类号：O62

摘要：Non-enzymatic glycation can cause the formation and accumulation of advanced glycation end products(AGEs),and it poses great threats to human health.It is urgent to search for safe and efficient inhibitors to prevent reducing sugar induced protein glycation.In this study,we inves-tigated the anti-glycation activity and mechanism of an identified peptide,Asparagine-Tyrosine-Arginine-Arginine-Glutamic acid(NYRRE)from Chinese quince seed protein hydrolysate,by mul-tispectroscopy,confocal imaging,and computational molecular simulation.Firstly,it was found that NYRRE could scavenge hydroxyl radicals and chelate Fe 2+.Besides,the NYRRE was effective in every stage of fructose induced bovine serum albumin(BSA)glycation.The NYRRE could re-duce the formation of fructosamine,carbonyl compounds,glycoxidation products and????-amyloid structure.Meanwhile,NYRRE could protect thiol groups and stabilize the spatial conformation of BSA.The NYRRE presented strong inhibition in fluorescent AGEs,and 68.19%of total AGEs formation was prevented with NYRRE at 15 mmol/L.The results of molecular simulation indi-cated that NYRRE could insert into the hydrophobic pocket of BSA and interact with hot spots,including arginine and lysine residues.The mechanism of NYRRE inhibiting protein glycation could be due to its antioxidant activity,BSA structure stabilizing ability,and specific bond with glycation sites of BSA.These results provided a valuable reference for developing NYRRE as an efficient antiglycation agent in preventing glycation-mediated diseases.