Spectroscopic analysis on the binding interaction of biologically active pyrimidine derivative with bovine serum albumin

作     者：Vishwas D. Suryawansht Laxman S. Walekar Anil H. Gore Prashant V. Anbhule Govind B. Kolekar 

作者机构：Fluorescence Spectroscopy Research Laboratory Department of Chemistry Shivaji University Kolhapur 416 004 Maharashtra India 

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

年 卷 期：2016年第6卷第1期

页      面：56-63页

核心收录：

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 070302[理学-分析化学] 0703[理学-化学] 

基　　金：receiving a fellowship from UGC New Delhi[University Grant Commission,the XIth plan(Faculty Improvement Programme)] DST and UGC for providing funds to the department under FIST and SAP programme 

主　　题：Bovine serum albumin Fluorescence spectroscopy Pyrimidine derivative Binding interaction Fluorescence resonance energy transfer(FRET) 

摘      要：A biologically active antibacterial reagent, 2-amino-6-hydroxy-4-（4-N, N-dimethylaminophenyl）-pyr- imidine-5-carbonitrile （AHDMAPPC）, was synthesized. It was employed to investigate the binding in- teraction with the bovine serum albumin （BSA） in detail using different spectroscopic methods. It ex- hibited antibacterial activity against Escherichia cali and Staphylococcus aureus which are common food poisoning bacteria. The experimental results showed that the fluorescence quenching of model carrier protein BSA by AHDMAPPC was due to static quenching. The site binding constants and number of binding sites （n ≈ 1） were determined at three different temperatures based on fluorescence quenching results. The thermodynamic parameters, enthalpy change （AH）, free energy （AG） and entropy change （AS） for the reaction were calculated to be 15.15 kJ/mol, -36.11 kJ/mol and 51.26J/mol K according to van＇t Hoff equation, respectively. The results indicated that the reaction was an endothermic and spontaneous process, and hydrophobic interactions played a major role in the binding between drug and BSA. The distance between donor and acceptor is 2.79 nm according to Forster＇s theory. The alterations of the BSA secondary structure in the presence of AHDMAPPC were confirmed by UV-visible, synchronous fluorescence, circular dichroism （CD） and three-dimensional fluorescence spectra. All these results in- dicated that AHDMAPPC can bind to BSA and be effectively transported and eliminated in the body. It can be a useful guideline for further drug design.