title: The binding properties of metandienone and human serum albumin by comparing with other five similar compounds.
abstract: Metandienone (MET) is an exogenous anabolic androgenic steroid. The interaction between MET and human serum albumin (HSA) was investigated by molecular modeling and different optical techniques. There was no possibility of energy transfer, and the fluorescence quenching of HSA induced by MET was mainly due to the complex formation. The differences of binding ability between MET and compounds 1-5 were significantly caused by space steric hindrance. The single crystallographic data of two steroids (compounds 4 and 5) were obtained in the methanol at the first time. In addition, the binding ability was slightly affected by -OH, -CH3, and -COCH3. The results of displacement experiment demonstrated that the MET binding site was mainly located in site 1 of HSA. H-bonding and van der Waals forces were significant in the MET-HSA binding. MET played an insignificant role on the local conformation change in HSA.
authors.affiliation: College of Chemical Engineering, Sichuan University, Chengdu, 610065, People's Republic of China.
authors.forename: Xiang
authors.initials: X
authors.lastname: Lin
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: Sinopharm Chuankang Pharmaceutical Co., Ltd., Chengdu, 611731, People's Republic of China.
authors.forename: Xilin
authors.initials: X
authors.lastname: Peng
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: D001665:Binding Sites; D002942:Circular Dichroism; D004735:Energy Transfer; D006801:Humans; D006860:Hydrogen Bonding; D008696:Methandrostenolone / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
chemical_list: D012709:Serum Albumin; D008696:Methandrostenolone
keywords: Binding ability; dansylsarcosine emission; human serum albumin (HSA); metandienone; warfarin emission