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This study investigated the interaction mechanism between SAF and HSA through multispectral techniques, molecular docking, and molecular dynamics simulations. The results show that SAF effectively reduces the intrinsic fluorescence of HSA through static quenching and forms a stable 1:1 molar ratio SAF\u2013HSA complex. SAF binds to the second domain site of HSA. The binding reaction is a spontaneous, exothermic process driven by enthalpy, mainly stabilized through hydrogen bonds and van der Waals forces. Spectral analysis confirmed an increase in the \u03b1\u2010helical structure of HSA upon binding. Molecular docking and molecular dynamics simulations, including analyses of RMSD, RMSF, and\n                    <jats:italic>R<\/jats:italic>\n                    g, further supported and elucidated the experimental results.\n                  <\/jats:p>","DOI":"10.1002\/cbdv.202503350","type":"journal-article","created":{"date-parts":[[2026,3,10]],"date-time":"2026-03-10T08:06:01Z","timestamp":1773129961000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Multispectral, Molecular Docking, and Dynamics Simulation Studies of Secalonic Acid F Binding to Human Serum Albumin"],"prefix":"10.1002","volume":"23","author":[{"given":"Jialing","family":"Shen","sequence":"first","affiliation":[{"name":"College of Materials and Energy South China Agricultural University  Guangzhou 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