title: Investigation on the Interaction of Norgestrel with Human Serum Albumin Using Spectroscopy and Molecular-Docking Method.
abstract: The interaction of norgestrel with human serum albumin (HSA) was investigated by spectroscopy and molecular-docking methods. 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 (ΔG, ΔH, and ΔS) indicated that hydrogen bonding and van der Waals forces dominated the binding between norgestrel and HSA. Three-dimensional 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-docking results. Competition among similar structures indicated that ethisterone and norethisterone affected the binding of norgestrel with HSA. CH3 in R1 had little effect on norgestrel binding with HSA. The surface hydrophobicity properties of HSA, investigated using 8-anilino-1-naphthalenesulfonic acid, was changed with norgestrel addition.
authors.affiliation: College of Chemical Engineering, Sichuan University, Chengdu, 610065, People's Republic of China. lihuilab@sina.com.
authors.forename: Xiangling
authors.initials: X
authors.lastname: Ma
authors.affiliation: College of Chemical Engineering, Sichuan University, Chengdu, 610065, People's Republic of China.
authors.forename: Qing
authors.initials: Q
authors.lastname: Wang
authors.affiliation: College of Chemical Engineering, Sichuan University, Chengdu, 610065, People's Republic of China.
authors.forename: Lili
authors.initials: L
authors.lastname: Wang
authors.affiliation: College of Chemical Engineering, Sichuan University, Chengdu, 610065, People's Republic of China.
authors.forename: Yanmei
authors.initials: Y
authors.lastname: Huang
authors.affiliation: College of Chemical Engineering, Sichuan University, Chengdu, 610065, People's Republic of China.|Technology Center, China Tobacco Yunnan Industrial Co, Ltd, Kunming, 650204, Yunnan, People's Republic of China.
authors.forename: Xiaoxiang
authors.initials: X
authors.lastname: Liao
authors.affiliation: College of Chemical Engineering, Sichuan University, Chengdu, 610065, People's Republic of China.
authors.forename: Hui
authors.initials: H
authors.lastname: Li
mesh_terms: D000817:Anilino Naphthalenesulfonates; D001665:Binding Sites; D003280:Contraceptives, Oral, Synthetic / Q000737:chemistry*; D005003:Ethisterone / Q000737:chemistry*; D005456:Fluorescent Dyes; D006801:Humans; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D062105:Molecular Docking Simulation; D009640:Norethindrone / Q000737:chemistry*; D009644:Norgestrel / Q000737:chemistry*; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*; D012996:Solutions; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
chemical_list: C515594:8-anilino-1-naphthalenesulfonic acid; D000817:Anilino Naphthalenesulfonates; D003280:Contraceptives, Oral, Synthetic; D005456:Fluorescent Dyes; D012709:Serum Albumin; D012996:Solutions; D009644:Norgestrel; D005003:Ethisterone; D009640:Norethindrone
keywords: 8-anilino-1-naphthalenesulfonic acid; Human Serum Albumin; Norgestrel; Similar Structures