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Spectroscopic analysis to identify the binding site for Rifampicin on Bovine Serum Albumin by Sudhanshu Sharma; Dineshbabu Takkella; Pintu Kumar; Krishna Gavvala is a Chemistry article available to read on EtoBox.

What is Spectroscopic analysis to identify the binding site for Rifampicin on Bovine Serum Albumin about?

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.

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

Author

Sudhanshu Sharma; Dineshbabu Takkella; Pintu Kumar; Krishna Gavvala

Publisher

Elsevier BV

Published

2022

Language

EN

Field

Chemistry (Physical Sciences)