{"title":"Generation of cyclic peptides with improved anti-Photoaging activity during the thermal processing of collagen peptides.","authors":"Wenxin Li, Danyin Yang, Lin Zheng, Mouming Zhao","doi":"10.1016/j.foodchem.2026.151561","DOIUrl":null,"url":null,"abstract":"<p><p>This study explored the structural changes of collagen peptides during heat treatment under different conditions that might affect their anti-photoaging activities. Results showed that the matrix metalloproteinase-1 (MMP-1) inhibition rate of collagen hydrolysates significantly increased after heat treatment at various pH values, and its contents of Hyp (O)-containing and Gly-Pro-Xaa tripeptides significantly reduced, while cyclic dipeptides such as cyclo(LO), cyclo(FO), and cyclo(GP) were formed. Specifically, cyclo(LO) and cyclo(GP) displayed stronger MMP-1 inhibition (64.12% and 52.81%, respectively) than the linear di- and tripeptides LO, LOG, GPI and GPM (35.86%, 22.03%, 21.28% and 41.14%, respectively). This might be due to their increased conformational rigidity and strengthened hydrophobic interactions with MMP-1. Additionally, the cyclic dipeptides cyclo(PO), cyclo(LO), cyclo(AO), cyclo(SO), cyclo(FO) and cyclo(GP) significantly enhanced the viability of fibroblasts damaged by UVA. The results highlighted the cyclic form of Hyp-containing dipeptides with improved anti-photoaging activity generated upon heat treatment and its potential application in skin health.</p>","PeriodicalId":318,"journal":{"name":"Food Chemistry","volume":"532 Pt 2","pages":"151561"},"PeriodicalIF":10.4000,"publicationDate":"2026-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Chemistry","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1016/j.foodchem.2026.151561","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
引用次数: 0
Abstract
This study explored the structural changes of collagen peptides during heat treatment under different conditions that might affect their anti-photoaging activities. Results showed that the matrix metalloproteinase-1 (MMP-1) inhibition rate of collagen hydrolysates significantly increased after heat treatment at various pH values, and its contents of Hyp (O)-containing and Gly-Pro-Xaa tripeptides significantly reduced, while cyclic dipeptides such as cyclo(LO), cyclo(FO), and cyclo(GP) were formed. Specifically, cyclo(LO) and cyclo(GP) displayed stronger MMP-1 inhibition (64.12% and 52.81%, respectively) than the linear di- and tripeptides LO, LOG, GPI and GPM (35.86%, 22.03%, 21.28% and 41.14%, respectively). This might be due to their increased conformational rigidity and strengthened hydrophobic interactions with MMP-1. Additionally, the cyclic dipeptides cyclo(PO), cyclo(LO), cyclo(AO), cyclo(SO), cyclo(FO) and cyclo(GP) significantly enhanced the viability of fibroblasts damaged by UVA. The results highlighted the cyclic form of Hyp-containing dipeptides with improved anti-photoaging activity generated upon heat treatment and its potential application in skin health.
期刊介绍:
Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.