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Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin 被引量:4
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作者 Manjunath D.Meti Sharanappa T.Nandibewoor +2 位作者 Shrinivas D.Joshi Uttam A.More shivamurti a.chimatadar 《Journal of Pharmaceutical Analysis》 SCIE CAS 2015年第4期249-255,共7页
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 ... 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. 展开更多
关键词 FosfomycinSerum albuminSpectroscopic methodsSynchronous fluorescence3D spectra
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