Studies on the binding of vinpocetine to human serum albumin by molecular spectroscopy and modeling  

作　　者：Hua Jiang Rong Rong Chen Hong Cui Wang Han Lin Pu 

机构地区：[1]Bio-engineering Institute,College of Life Science and Technology,Jinan University,Guangzhou 510632,China

出　　处：《Chinese Chemical Letters》2012年第5期599-602,共4页中国化学快报（英文版）

摘　　要：The interaction between vinpocetine（VPC） and human serum albumin（HSA） in physiological buffer（pH 7.40） was investigated by fluorescence,FT-IR,UV-vis absorption and molecular modeling.VPC effectively quenched the intrinsic fluorescence of HSA via static quenching.The binding site number n and apparent binding constant K_a,corresponding thermodynamic parametersΔG,ΔH andΔS at different temperatures were calculated.The synchronous fluorescence and FT-IR spectra were used to investigate the structural change of HSA molecules with addition of VPC.Molecular modeling indicated that VPC could bind to the site I of HSA and hydrophobic interaction was the major acting force,which was in agreement with the binding mode study.The interaction between vinpocetine（VPC） and human serum albumin（HSA） in physiological buffer（pH 7.40） was investigated by fluorescence,FT-IR,UV-vis absorption and molecular modeling.VPC effectively quenched the intrinsic fluorescence of HSA via static quenching.The binding site number n and apparent binding constant K_a,corresponding thermodynamic parametersΔG,ΔH andΔS at different temperatures were calculated.The synchronous fluorescence and FT-IR spectra were used to investigate the structural change of HSA molecules with addition of VPC.Molecular modeling indicated that VPC could bind to the site I of HSA and hydrophobic interaction was the major acting force,which was in agreement with the binding mode study.

关 键 词：VINPOCETINE Human serum albumin Fluorescence quenching Molecular modeling 

分 类 号：O561.3[理学—原子与分子物理] Q512.1[理学—物理]