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The pharmacokinetics and pharmacodynamics properties of a drug could be understood via study its mechanism of interaction with bovine serum albumin protein (BSA). Therefore, the\u00a0interaction between\u00a0MiADMSA with BSA was investigated\u00a0using various spectroscopic techniques and computational methods. Linear quenching of BSA intrinsic fluorescence intensity with the increasing concentration of MiADMSA was observed in the\u00a0fluorescence study. Furthermore, synchronous results revealed that MiADMSA slightly changed the conformation of BSA. The binding constant value of the BSA-MiADMSA complex was found 1.60\u2009\u00d7\u200910<jats:sup>4<\/jats:sup>\u00a0M<jats:sup>\u22121<\/jats:sup> at 298\u00a0K. The value of thermodynamic parameters \u0394G, \u0394H, and \u0394S described that the process is spontaneous, endothermic, and hydrophobic forces are involved in the interaction of MiADMSA with BSA. Competitive site marker experiments showed that MiADMSA binds to site-II of BSA. Conformational changes of BSA with the interaction of MiADMSA were apparent by CD, UV\u2013Visible, FT-IR, and 3D fluorescence spectroscopy. To strengthen the experimental findings we have also performed a theoretical study on the BSA-MiADMSA complex. Two sites were identified with docking score of\u2009\u2212\u20096.642\u00a0kcal\/mol at site II<jats:sub>a<\/jats:sub> and\u2009\u2212\u20093.80\u00a0kcal\/mol for site II<jats:sub>b<\/jats:sub> via molecular docking study. Molecular dynamics simulation study inferred the stability of the\u00a0BSA-MiADMSA complex which was analyzed in\u00a0a long simulation run. The experimental and computational studies have shown the effective binding of MiADMSA with BSA which is essential for\u00a0the transportation and elimination of a\u00a0drug from the body.<\/jats:p>","DOI":"10.1038\/s41598-021-83534-0","type":"journal-article","created":{"date-parts":[[2021,2,20]],"date-time":"2021-02-20T09:14:59Z","timestamp":1613812499000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["Interaction study of monoisoamyl dimercaptosuccinic acid with bovine serum albumin using biophysical and molecular docking approaches"],"prefix":"10.1038","volume":"11","author":[{"given":"Ashima","family":"Thakur","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jayant","family":"Patwa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suyash","family":"Pant","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Abha","family":"Sharma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S. 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