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In\u2010depth research on their interactions with serum albumin can enhance their bioavailability and\n                      <jats:italic>in vivo<\/jats:italic>\n                      functionality from functional food.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>RESULTS<\/jats:title>\n                    <jats:p>This study systematically investigated the impact of the ACEIP Gly\u2010Arg\u2010Pro (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\u2010converting enzyme inhibitory activity and had good biosafety in cytotoxicity assays. Steady\u2010state and time\u2010resolved fluorescence spectroscopy indicated the formation of a moderately bound BSA\u2013GRP complex in various buffer environments. The existence of the BSA\u2013GRP complex was further confirmed by ultraviolet\u2013visible spectroscopy. Three\u2010dimensional 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.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>CONCLUSION<\/jats:title>\n                    <jats:p>This work established a research system for BSA\u2013GRP interactions and obtained relevant parameters, which will benefit the subsequent development of nutritional supplements and functional foods. \u00a9 2025 Society of Chemical Industry.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1002\/jsfa.70048","type":"journal-article","created":{"date-parts":[[2025,7,11]],"date-time":"2025-07-11T18:03:32Z","timestamp":1752257012000},"page":"8014-8026","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["In\u2010depth analysis of dynamic binding of sardine\u2010derived functional tripeptide with serum albumin in diverse buffers"],"prefix":"10.1002","volume":"105","author":[{"given":"Lei","family":"Wang","sequence":"first","affiliation":[{"name":"School of Medicine, and Guangxi Key Laboratory of Petrochemical Resource Processing and Process Intensification Technology, School of Chemistry and Chemical Engineering Guangxi University  Nanning China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dankui","family":"Liao","sequence":"additional","affiliation":[{"name":"School of Medicine, and Guangxi Key Laboratory of Petrochemical Resource Processing and Process Intensification Technology, School of Chemistry and Chemical Engineering Guangxi University  Nanning China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Qian","family":"Zhou","sequence":"additional","affiliation":[{"name":"School of Medicine, and Guangxi Key Laboratory of Petrochemical Resource Processing and Process Intensification Technology, School of Chemistry and Chemical Engineering Guangxi University  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