Spectroscopic analysis to identify the binding site for Rifampicin on Bovine Serum Albumin

Sharma, Sudhanshu and Takkella, Dineshbabu and Kumar, Pintu and Gavvala, Krishna (2022) Spectroscopic analysis to identify the binding site for Rifampicin on Bovine Serum Albumin. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 283. pp. 1-6. ISSN 1386-1425

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Abstract

This article reports the interaction of rifampicin, one of the important antituberculosis drugs, with Bovine Serum Albumin (BSA). Herein, we have monitored the fluorescence properties of tryptophan (Trp) residue in BSA to understand the interactions between protein and rifampicin. Fluorescence intensity of BSA was quenched tremendously upon interacting with the drug. Using steady state and time-resolved spectroscopic tools the static and dynamic nature of quenching have been characterised. Time correlated single photon counting technique confirmed that out of two lifetime components ∼6.2 ns and ∼2.8 ns of BSA, the rifampicin has affected only the shorter lifetime component a lot that was assigned to Trp-213 residue. Hence, it was thought that the drug must have been located near to the amino acid residue. Molecular docking studies have revealed the structural information of drug-protein complex which supported the above conjecture, confirming the nearest tryptophan as Trp-213 to the complexing rifampicin molecule. © 2022 Elsevier B.V.

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IITH Creators:
IITH CreatorsORCiD
Gavvala, KrishnaUNSPECIFIED
Item Type: Article
Additional Information: K.G. is thankful to the Science and Engineering Research Board (SERB), Government of India for the start-up research grant (SRG/2020/000248). D.T. and S.S. are thankful to the University Grants Commission (UGC) for the research fellowship. Authors thank Indian Institute of Technology (IIT) Hyderabad for providing the research facilities.
Uncontrolled Keywords: Antituberculosis drug; Bovine serum albumin; Fluorescence decay; Fluorescence emission; Rifampicin; Stern–volmer constant
Subjects: Chemistry
Divisions: Department of Chemistry
Depositing User: . LibTrainee 2021
Date Deposited: 18 Oct 2022 05:00
Last Modified: 18 Oct 2022 05:00
URI: http://raiithold.iith.ac.in/id/eprint/10992
Publisher URL: http://doi.org/10.1016/j.saa.2022.121721
OA policy: https://v2.sherpa.ac.uk/id/publication/15140
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