文献类型：期刊文献

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

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

第一作者：邓叶俊

通信作者：Huang, LX[1];Huang, LX[2]

机构：[1]Chinese Acad Forestry, Inst Chem Ind Forest Prod, Natl Engn Lab Biomass Chem Utilizat, Key & Open Lab Forest Chem Engn,Natl Forestry & Gr, Nanjing 210042, Jiangsu, Peoples R China;[2]Nanjing Forestry Univ, Coinnovat Ctr Efficient Proc & Utilizat Forest Res, Nanjing 210037, Peoples R China

年份：2023

卷号：8

期号：2

起止页码：187-197

外文期刊名：JOURNAL OF BIORESOURCES AND BIOPRODUCTS

收录：;EI(收录号：20230513493141);Scopus(收录号：2-s2.0-85147112289);WOS:【SCI-EXPANDED(收录号:WOS:000996049800001)，ESCI(收录号:WOS:000996049800001)】；

基金：The authors are grateful for the financial support for this work by National Natural Science Foundation of China (No. 32171732) . The authors acknowledge all people for their contributions to this study, and specially appreciate Professor Fang Xin from Kunming Institute of botany, Chinese academy of sciences, for his kind software support.

语种：英文

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

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 investigated the anti-glycation activity and mechanism of an identified peptide, Asparagine-Tyrosine-Arginine-Arginine-Glutamic acid (NYRRE) from Chinese quince seed protein hydrolysate, by multispectroscopy, confocal imaging, and computational molecular simulation. Firstly, it was found that NYRRE could scavenge hydroxyl radicals and chelate Fe2+. Besides, the NYRRE was effective in every stage of fructose induced bovine serum albumin (BSA) glycation. The NYRRE could reduce the formation of fructosamine, carbonyl compounds, glycoxidation products and beta-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 indicated 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.