罗非鱼皮肤胶原蛋白中强效二肽基肽酶IV（DPP-IV）抑制肽的释放模式

IF 9.8 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Chemistry Pub Date : 2025-05-28 DOI:10.1016/j.foodchem.2025.144970

Jiaxin Li , Danyin Yang , Qiongyao Xu , Mingtao Huang , Lin Zheng , Mouming Zhao

{"title":"罗非鱼皮肤胶原蛋白中强效二肽基肽酶IV（DPP-IV）抑制肽的释放模式","authors":"Jiaxin Li , Danyin Yang , Qiongyao Xu , Mingtao Huang , Lin Zheng , Mouming Zhao","doi":"10.1016/j.foodchem.2025.144970","DOIUrl":null,"url":null,"abstract":"<div><div>Gly-Pro-type peptides consisting of 4–9 amino acids are the most potent DPP-IV inhibitory peptides in collagen. In this study, we investigated the release patterns of collagen-derived Gly-Pro-type peptides with DPP-IV inhibitory activities by analyzing the cleavage selectivity of proteases, and the dynamic release mechanism of Gly-Pro-type peptides. Results showed that collagen hydrolysate with the highest DPP-IV inhibitory activity was obtained by proteaC (IC<sub>50</sub> = 0.58 ± 0.02 mg/mL). Large amounts of Gly-Pro-type peptides consisting of 4, 6, and 9 amino acids were released. ProteaC preferred to cleave Gly and hydrophobic amino acids residues at the P1’ position, and had a strong cleavage preference for Hyp residue at the P1 position. The dynamic release mode indicated that the release of potent DPP-IV inhibitory peptides underwent a change from precursor peptides to target peptides and then to short peptides. These findings provided a better understanding of the release of DPP-IV inhibitory peptides.</div></div>","PeriodicalId":318,"journal":{"name":"Food Chemistry","volume":"489 ","pages":"Article 144970"},"PeriodicalIF":9.8000,"publicationDate":"2025-05-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Release pattern of potent dipeptidyl peptidase IV(DPP-IV) inhibitory peptides from tilapia (Oreochromis niloticus) skin collagen\",\"authors\":\"Jiaxin Li , Danyin Yang , Qiongyao Xu , Mingtao Huang , Lin Zheng , Mouming Zhao\",\"doi\":\"10.1016/j.foodchem.2025.144970\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Gly-Pro-type peptides consisting of 4–9 amino acids are the most potent DPP-IV inhibitory peptides in collagen. In this study, we investigated the release patterns of collagen-derived Gly-Pro-type peptides with DPP-IV inhibitory activities by analyzing the cleavage selectivity of proteases, and the dynamic release mechanism of Gly-Pro-type peptides. Results showed that collagen hydrolysate with the highest DPP-IV inhibitory activity was obtained by proteaC (IC<sub>50</sub> = 0.58 ± 0.02 mg/mL). Large amounts of Gly-Pro-type peptides consisting of 4, 6, and 9 amino acids were released. ProteaC preferred to cleave Gly and hydrophobic amino acids residues at the P1’ position, and had a strong cleavage preference for Hyp residue at the P1 position. The dynamic release mode indicated that the release of potent DPP-IV inhibitory peptides underwent a change from precursor peptides to target peptides and then to short peptides. These findings provided a better understanding of the release of DPP-IV inhibitory peptides.</div></div>\",\"PeriodicalId\":318,\"journal\":{\"name\":\"Food Chemistry\",\"volume\":\"489 \",\"pages\":\"Article 144970\"},\"PeriodicalIF\":9.8000,\"publicationDate\":\"2025-05-28\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Chemistry\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0308814625022216\",\"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}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Chemistry","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0308814625022216","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

摘要

由4-9个氨基酸组成的gly - pro型肽是胶原中最有效的DPP-IV抑制肽。本研究通过分析蛋白酶的裂解选择性，探讨具有DPP-IV抑制活性的胶原源性gly - pro型多肽的释放模式，以及gly - pro型多肽的动态释放机制。结果表明，用proteaC制备的胶原水解液抑制DPP-IV活性最高（IC50 = 0.58 ± 0.02 mg/mL）。大量由4、6和9个氨基酸组成的gly - pro型肽被释放。ProteaC倾向于切割P1 '位置的Gly和疏水氨基酸残基，而对P1位置的Hyp残基具有强烈的切割偏好。动态释放模式表明，DPP-IV强效抑制肽的释放经历了从前体肽到靶肽再到短肽的变化。这些发现为DPP-IV抑制肽的释放提供了更好的理解。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

查看原文本刊更多论文

Release pattern of potent dipeptidyl peptidase IV(DPP-IV) inhibitory peptides from tilapia (Oreochromis niloticus) skin collagen

Gly-Pro-type peptides consisting of 4–9 amino acids are the most potent DPP-IV inhibitory peptides in collagen. In this study, we investigated the release patterns of collagen-derived Gly-Pro-type peptides with DPP-IV inhibitory activities by analyzing the cleavage selectivity of proteases, and the dynamic release mechanism of Gly-Pro-type peptides. Results showed that collagen hydrolysate with the highest DPP-IV inhibitory activity was obtained by proteaC (IC₅₀ = 0.58 ± 0.02 mg/mL). Large amounts of Gly-Pro-type peptides consisting of 4, 6, and 9 amino acids were released. ProteaC preferred to cleave Gly and hydrophobic amino acids residues at the P1’ position, and had a strong cleavage preference for Hyp residue at the P1 position. The dynamic release mode indicated that the release of potent DPP-IV inhibitory peptides underwent a change from precursor peptides to target peptides and then to short peptides. These findings provided a better understanding of the release of DPP-IV inhibitory peptides.

求助全文

通过发布文献求助，成功后即可免费获取论文全文。去求助

来源期刊

Food Chemistry 工程技术-食品科技

CiteScore

16.30

自引率

10.20%

发文量

3130

审稿时长

122 days

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.