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Results of spectroscopy methods suggested that the quenching mechanism of norgestrel on HSA was static quenching and that the quenching process was spontaneous. Negative values of thermodynamic parameters (\u0394<jats:italic>G<\/jats:italic>, \u0394<jats:italic>H<\/jats:italic>, and \u0394<jats:italic>S<\/jats:italic>) indicated that hydrogen bonding and van der Waals forces dominated the binding between norgestrel and HSA. Three\u2010dimensional fluorescence spectrum and circular dichroism spectrum showed that the HSA structure was slightly changed by norgestrel. Norgestrel mainly bound with Sudlow site I based on a probe study, as confirmed by molecular\u2010docking results. Competition among similar structures indicated that ethisterone and norethisterone affected the binding of norgestrel with HSA. CH<jats:sub>3<\/jats:sub> in R<jats:sub>1<\/jats:sub> had little effect on norgestrel binding with HSA. The surface hydrophobicity properties of HSA, investigated using 8\u2010anilino\u20101\u2010naphthalenesulfonic acid, was changed with norgestrel addition.<\/jats:p>","DOI":"10.1002\/jbt.21790","type":"journal-article","created":{"date-parts":[[2016,1,18]],"date-time":"2016-01-18T07:50:16Z","timestamp":1453103416000},"page":"287-294","source":"Crossref","is-referenced-by-count":9,"title":["Investigation on the Interaction of Norgestrel with Human Serum Albumin Using Spectroscopy and Molecular\u2010Docking Method"],"prefix":"10.1002","volume":"30","author":[{"given":"Xiangling","family":"Ma","sequence":"first","affiliation":[{"name":"College of Chemical Engineering Sichuan University  Chengdu 610065 People's Republic of China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Qing","family":"Wang","sequence":"additional","affiliation":[{"name":"College of Chemical Engineering Sichuan University  Chengdu 610065 People's Republic of 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