In-depth analysis of dynamic binding of sardine-derived functional tripeptide with serum albumin in diverse buffers.

IF 3.3 2区农林科学 Q1 AGRICULTURE, MULTIDISCIPLINARY

Journal of the Science of Food and Agriculture Pub Date : 2025-07-11 DOI:10.1002/jsfa.70048

Lei Wang, Dankui Liao, Qian Zhou, Lixia Sun, Xueping Zhang, Xiongdiao Lan, Zhangfa Tong, Meiqun Suo, Guangzhi Zhou

{"title":"In-depth analysis of dynamic binding of sardine-derived functional tripeptide with serum albumin in diverse buffers.","authors":"Lei Wang, Dankui Liao, Qian Zhou, Lixia Sun, Xueping Zhang, Xiongdiao Lan, Zhangfa Tong, Meiqun Suo, Guangzhi Zhou","doi":"10.1002/jsfa.70048","DOIUrl":null,"url":null,"abstract":"Background: Food-derived angiotensin-converting enzyme inhibitory peptides (ACEIPs) are commonly utilized in functional food development. In-depth research on their interactions with serum albumin can enhance their bioavailability and in vivo functionality from functional food.Results: This study systematically investigated the impact of the ACEIP Gly-Arg-Pro (GRP) derived from sardine muscle protein on the conformation and interaction mechanisms of bovine serum albumin (BSA) under different physiological buffer environments using multispectral techniques, molecular docking theory and isothermal titration calorimetry. GRP demonstrated potent angiotensin-converting enzyme inhibitory activity and had good biosafety in cytotoxicity assays. Steady-state and time-resolved fluorescence spectroscopy indicated the formation of a moderately bound BSA-GRP complex in various buffer environments. The existence of the BSA-GRP complex was further confirmed by ultraviolet-visible spectroscopy. Three-dimensional fluorescence spectroscopy, synchronous fluorescence spectroscopy and circular dichroism spectroscopy demonstrated that adding GRP to BSA affected its microenvironment and structural conformation, with more significant changes observed in the HEPES buffer system due to its distinct physicochemical properties. The thermodynamic parameters indicated that the interaction was mainly driven by hydrophobic forces, making it a spontaneous process regarding Gibbs free energy change. Molecular docking theory showed that GRP is preferentially bound to site II of subdomain IIIA.Conclusion: This work established a research system for BSA-GRP interactions and obtained relevant parameters, which will benefit the subsequent development of nutritional supplements and functional foods. © 2025 Society of Chemical Industry.","PeriodicalId":17725,"journal":{"name":"Journal of the Science of Food and Agriculture","volume":" ","pages":""},"PeriodicalIF":3.3000,"publicationDate":"2025-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of the Science of Food and Agriculture","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1002/jsfa.70048","RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURE, MULTIDISCIPLINARY","Score":null,"Total":0}

引用次数: 0

Abstract

Background: Food-derived angiotensin-converting enzyme inhibitory peptides (ACEIPs) are commonly utilized in functional food development. In-depth research on their interactions with serum albumin can enhance their bioavailability and in vivo functionality from functional food.

Results: This study systematically investigated the impact of the ACEIP Gly-Arg-Pro (GRP) derived from sardine muscle protein on the conformation and interaction mechanisms of bovine serum albumin (BSA) under different physiological buffer environments using multispectral techniques, molecular docking theory and isothermal titration calorimetry. GRP demonstrated potent angiotensin-converting enzyme inhibitory activity and had good biosafety in cytotoxicity assays. Steady-state and time-resolved fluorescence spectroscopy indicated the formation of a moderately bound BSA-GRP complex in various buffer environments. The existence of the BSA-GRP complex was further confirmed by ultraviolet-visible spectroscopy. Three-dimensional fluorescence spectroscopy, synchronous fluorescence spectroscopy and circular dichroism spectroscopy demonstrated that adding GRP to BSA affected its microenvironment and structural conformation, with more significant changes observed in the HEPES buffer system due to its distinct physicochemical properties. The thermodynamic parameters indicated that the interaction was mainly driven by hydrophobic forces, making it a spontaneous process regarding Gibbs free energy change. Molecular docking theory showed that GRP is preferentially bound to site II of subdomain IIIA.

Conclusion: This work established a research system for BSA-GRP interactions and obtained relevant parameters, which will benefit the subsequent development of nutritional supplements and functional foods. © 2025 Society of Chemical Industry.

查看原文本刊更多论文

深入分析沙丁鱼衍生的功能性三肽与不同缓冲液中血清白蛋白的动态结合。

背景：食源性血管紧张素转换酶抑制肽（ACEIPs）在功能性食品开发中被广泛应用。深入研究它们与血清白蛋白的相互作用，可以提高它们在功能食品中的生物利用度和体内功能。结果：本研究采用多光谱技术、分子对接理论和等温滴定量热法，系统研究了不同生理缓冲环境下沙丁鱼肌蛋白衍生ACEIP Gly-Arg-Pro （GRP）对牛血清白蛋白（BSA）构象的影响及其相互作用机制。GRP在细胞毒性试验中表现出较强的血管紧张素转换酶抑制活性，具有良好的生物安全性。稳态和时间分辨荧光光谱表明，在不同的缓冲环境中形成了中等结合的BSA-GRP复合物。紫外-可见光谱进一步证实了BSA-GRP配合物的存在。三维荧光光谱、同步荧光光谱和圆二色光谱分析表明，GRP加入BSA会影响其微环境和结构构象，其中HEPES缓冲体系由于其独特的物理化学性质，其变化更为显著。热力学参数表明，相互作用主要由疏水力驱动，是一个自发的吉布斯自由能变化过程。分子对接理论表明，GRP优先结合到IIIA亚结构域的II位点。结论：本工作建立了BSA-GRP相互作用的研究体系，并获得了相关参数，为后续营养补充剂和功能食品的开发提供了依据。©2025化学工业协会。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文求助全文

来源期刊

Journal of the Science of Food and Agriculture 工程技术-农业综合

CiteScore

8.10

自引率

4.90%

发文量

634

审稿时长

3.1 months

期刊介绍： The Journal of the Science of Food and Agriculture publishes peer-reviewed original research, reviews, mini-reviews, perspectives and spotlights in these areas, with particular emphasis on interdisciplinary studies at the agriculture/ food interface. Published for SCI by John Wiley & Sons Ltd. SCI (Society of Chemical Industry) is a unique international forum where science meets business on independent, impartial ground. Anyone can join and current Members include consumers, business people, environmentalists, industrialists, farmers, and researchers. The Society offers a chance to share information between sectors as diverse as food and agriculture, pharmaceuticals, biotechnology, materials, chemicals, environmental science and safety. As well as organising educational events, SCI awards a number of prestigious honours and scholarships each year, publishes peer-reviewed journals, and provides Members with news from their sectors in the respected magazine, Chemistry & Industry . Originally established in London in 1881 and in New York in 1894, SCI is a registered charity with Members in over 70 countries.