Multi-spectroscopic characterization of bovine serum albumin upon interaction with atomoxetine

作     者：Arunkumar T. Buddanavar Sharanappa T. Nandibewoor 

作者机构：P.G. Department of studies in ChemistryKarnatak UniversityDharwad 580003India 

出 版 物：《Journal of Pharmaceutical Analysis》 (药物分析学报（英文版）)

年 卷 期：2017年第7卷第3期

页      面：148-155页

核心收录：

学科分类：0710[理学-生物学] 1007[医学-药学(可授医学、理学学位)] 1006[医学-中西医结合] 100706[医学-药理学] 1002[医学-临床医学] 0817[工学-化学工程与技术] 0703[理学-化学] 0702[理学-物理学] 100602[医学-中西医结合临床] 10[医学] 

基　　金：Karnatak University, Dharwad, India, for providing UGC-UPE fellowship UGC, New Delhi for the award of BSR Faculty Fellowship (F No.18-1/2011) to Prof. S.T. Nandibewoor 

主　　题：Atomoxetine Bovine serum albumin 3D fluorescence spectra FT-IR Energy transfer Lifetime measurement 

摘      要：The quenching interaction of atomoxetine(ATX) with bovine serum albumin(BSA) was studied in vitro under optimal physiological condition(pH=7.4) by multi-spectroscopic techniques. The mechanism of ATX-BSA system was a dynamic quenching process and was confirmed by the fluorescence spectra and lifetime measurements. The number of binding sites, binding constants and other binding characteristics were computed. Thermodynamic parameters ΔH^0 and ΔS^0 indicated that intermolecular hydrophobic forces predominantly stabilized the drug-protein system. The average binding distance between BSA and ATX was studied by F?rsters theory. UV-absorption, Fourier transform infrared spectroscopy(FT-IR), circular dichroism(CD), synchronous spectra and three-dimensional(3D) fluorescence spectral results revealed the changes in micro-environment of secondary structure of protein upon the interaction with ATX. Displacement of site probes and the effects of some common metal ions on the binding of ATX with BSA interaction were also studied.