Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin  

作　　者：Manjunath D.Meti Sharanappa T.Nandibewoor Shrinivas D.Joshi Uttam A.More Shivamurti A.Chimatadar 

机构地区：[1]Post Graduate Department of Studies in Chemistry, Karnatak University, Pavate Nagar, Dharwad 580003, Karnataka, India [2]Novel Drug Design and Discovery Laboratory, Department of Pharmaceutical Chemistry, S.E.T’s College of Pharmacy, Sangolli Rayanna Nagar,Dharwad 580002, Karnataka, India

出　　处：《Journal of Pharmaceutical Analysis》2015年第4期249-255,共7页药物分析学报（英文版）

基　　金：DST New Delhi for providing Innovation in Science Pursuit for Inspired Research (INSPIRE) fellowship (IF110548)

摘　　要：The interaction between fosfomycin （FOS） and bovine serum albumin （BSA） has been investigated ef- fectively by multi-spectroscopic techniques under physiological pH 7.4. FOS quenched the intrinsic fluorescence of BSA via static quenching. The number of binding sites n and observed binding constant KA were measured by the fluorescence quenching method. The thermodynamic parameters AG0, AH0 and △S0 were calculated at different temperatures according to the van＇t Hoff equation. The site of binding of FOS in the protein was proposed to be Sudlow＇s site I based on displacement experiments using site markers viz. warfarin, ibuprofen and digitoxin. The distance r between the donor （BSA） and acceptor （FOS） molecules was obtained according to the F^rster theory. The effect of FOS on the conformation of BSA was analyzed using synchronous fluorescence spectra （SFS）, circular dichroism （CD） and 3D fluor- escence spectra. A molecular modeling study further confirmed the binding mode obtained by the ex- perimental studies.The interaction between fosfomycin （FOS） and bovine serum albumin （BSA） has been investigated ef- fectively by multi-spectroscopic techniques under physiological pH 7.4. FOS quenched the intrinsic fluorescence of BSA via static quenching. The number of binding sites n and observed binding constant KA were measured by the fluorescence quenching method. The thermodynamic parameters AG0, AH0 and △S0 were calculated at different temperatures according to the van＇t Hoff equation. The site of binding of FOS in the protein was proposed to be Sudlow＇s site I based on displacement experiments using site markers viz. warfarin, ibuprofen and digitoxin. The distance r between the donor （BSA） and acceptor （FOS） molecules was obtained according to the F^rster theory. The effect of FOS on the conformation of BSA was analyzed using synchronous fluorescence spectra （SFS）, circular dichroism （CD） and 3D fluor- escence spectra. A molecular modeling study further confirmed the binding mode obtained by the ex- perimental studies.

关 键 词：FosfomycinSerum albuminSpectroscopic methodsSynchronous fluorescence3D spectra 

分 类 号：R96[医药卫生—药理学]