Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin
The interaction between fosfomycin (FOS) and bovine serum albumin (BSA) has been investigated effectively 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...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2015-08-01
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| Series: | Journal of Pharmaceutical Analysis |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2095177915000167 |
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| author | Manjunath D. Meti Sharanappa T. Nandibewoor Shrinivas D. Joshi Uttam A. More Shivamurti A. Chimatadar |
| author_facet | Manjunath D. Meti Sharanappa T. Nandibewoor Shrinivas D. Joshi Uttam A. More Shivamurti A. Chimatadar |
| author_sort | Manjunath D. Meti |
| collection | DOAJ |
| description | The interaction between fosfomycin (FOS) and bovine serum albumin (BSA) has been investigated effectively 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 ÎG0, ÎH0 and ÎS0 were calculated at different temperatures according to the vanât Hoff equation. The site of binding of FOS in the protein was proposed to be Sudlowâs 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 Förster theory. The effect of FOS on the conformation of BSA was analyzed using synchronous fluorescence spectra (SFS), circular dichroism (CD) and 3D fluorescence spectra. A molecular modeling study further confirmed the binding mode obtained by the experimental studies. Keywords: Fosfomycin, Serum albumin, Spectroscopic methods, Synchronous fluorescence, 3D spectra |
| first_indexed | 2024-12-22T06:59:37Z |
| format | Article |
| id | doaj.art-ed95592838434bd09f6b60e905370d66 |
| institution | Directory Open Access Journal |
| issn | 2095-1779 |
| language | English |
| last_indexed | 2024-12-22T06:59:37Z |
| publishDate | 2015-08-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Pharmaceutical Analysis |
| spelling | doaj.art-ed95592838434bd09f6b60e905370d662022-12-21T18:34:51ZengElsevierJournal of Pharmaceutical Analysis2095-17792015-08-0154249255Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albuminManjunath D. Meti0Sharanappa T. Nandibewoor1Shrinivas D. Joshi2Uttam A. More3Shivamurti A. Chimatadar4Post Graduate Department of Studies in Chemistry, Karnatak University, Pavate Nagar, Dharwad 580003, Karnataka, IndiaPost Graduate Department of Studies in Chemistry, Karnatak University, Pavate Nagar, Dharwad 580003, Karnataka, IndiaNovel Drug Design and Discovery Laboratory, Department of Pharmaceutical Chemistry, S.E.Tâs College of Pharmacy, Sangolli Rayanna Nagar, Dharwad 580002, Karnataka, IndiaNovel Drug Design and Discovery Laboratory, Department of Pharmaceutical Chemistry, S.E.Tâs College of Pharmacy, Sangolli Rayanna Nagar, Dharwad 580002, Karnataka, IndiaPost Graduate Department of Studies in Chemistry, Karnatak University, Pavate Nagar, Dharwad 580003, Karnataka, India; Corresponding author. Tel.: +91 836 2215286; fax: +91 836 2747884.The interaction between fosfomycin (FOS) and bovine serum albumin (BSA) has been investigated effectively 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 ÎG0, ÎH0 and ÎS0 were calculated at different temperatures according to the vanât Hoff equation. The site of binding of FOS in the protein was proposed to be Sudlowâs 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 Förster theory. The effect of FOS on the conformation of BSA was analyzed using synchronous fluorescence spectra (SFS), circular dichroism (CD) and 3D fluorescence spectra. A molecular modeling study further confirmed the binding mode obtained by the experimental studies. Keywords: Fosfomycin, Serum albumin, Spectroscopic methods, Synchronous fluorescence, 3D spectrahttp://www.sciencedirect.com/science/article/pii/S2095177915000167 |
| spellingShingle | Manjunath D. Meti Sharanappa T. Nandibewoor Shrinivas D. Joshi Uttam A. More Shivamurti A. Chimatadar Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin Journal of Pharmaceutical Analysis |
| title | Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin |
| title_full | Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin |
| title_fullStr | Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin |
| title_full_unstemmed | Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin |
| title_short | Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin |
| title_sort | multi spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin |
| url | http://www.sciencedirect.com/science/article/pii/S2095177915000167 |
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