title: [Interaction between ambroxol hydrochloride and human serum albumin studied by spectroscopic and molecular modeling methods].
abstract: In the present paper, the interaction between ambroxol hydrochloride (ABX) and human serum albumin (HSA) was studied under simulative physiological condition by spectroscopy and molecular modeling method. Stern-Volmer curvers at different temperatures and UV-Vis absorption spectroscopy showed that ABX quenched the fluorescence of HSA mainly through dynamic quenching mode. On the basis of the thermodynamic data, the main binding force between them is hydrophobic interaction. According to the theory of Forster non-radiation energy transfer, the binding distance between the donor and the acceptor was 3.01 nm. The effect of ABX on the conformation of HSA was analyzed by the synchronous and three-dimensional fluorescence spectroscopy. Furthermore, using the molecular modeling method, the interaction between them was predicted from molecular angle: ABX might locate in the subdomain III A of HSA.
authors.affiliation: College of Chemistry and Environmental Science, Henan Normal University, Xinxiang 453007, China. jingl.2009@163.com
authors.forename: Jing
authors.initials: J
authors.lastname: Liang
authors.forename: Su-Ling
authors.initials: SL
authors.lastname: Feng
mesh_terms: D000551:Ambroxol; D004735:Energy Transfer; D005453:Fluorescence; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008968:Molecular Conformation; D012709:Serum Albumin; D013050:Spectrometry, Fluorescence; D013057:Spectrum Analysis; D013816:Thermodynamics
chemical_list: D012709:Serum Albumin; D000551:Ambroxol