Study on the interaction between anti‐tuberculosis drug ethambutol and bovine serum albumin: multispectroscopic and cyclic voltammetric approaches

The binding of bovine serum albumin (BSA) to ethambutol (EMB) was investigated using spectroscopic methods, viz., fluorescence, Fourier transform infrared (FTIR), ultraviolet (UV)/vis absorption and cyclic voltammetry techniques. Spectroscopic analysis of the emission quenching at different temperat...

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Bibliographic Details
Published in:Luminescence (Chichester, England) England), 2017-03, Vol.32 (2), p.206-216
Main Authors: Magdum, Prashant A., Gokavi, Naveen M., Nandibewoor, Sharanappa T.
Format: Article
Language:English
Subjects:
3D fluorescence spectrum
Absorption
Animals
Antitubercular Agents - chemistry
bovine serum albumin
Cattle
cyclic voltammetry
Electrochemical Techniques
ethambutol
Ethambutol - chemistry
Fluorescence
fluorescence quenching
Fourier transforms
Infrared spectroscopy
Mathematical analysis
protein binding
Quenching
Serum albumin
Serum Albumin, Bovine - chemistry
Spectra
Spectrometry, Fluorescence
Spectrophotometry, Ultraviolet
Spectroscopy, Fourier Transform Infrared
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Summary:The binding of bovine serum albumin (BSA) to ethambutol (EMB) was investigated using spectroscopic methods, viz., fluorescence, Fourier transform infrared (FTIR), ultraviolet (UV)/vis absorption and cyclic voltammetry techniques. Spectroscopic analysis of the emission quenching at different temperatures revealed that the quenching mechanism of serum albumin by EMB is static, which was also confirmed by lifetime measurements. The number of binding sites, n, and binding constant, K, were obtained at various temperatures. The distance, r, between EMB and the protein was evaluated according to the Förster energy transfer theory. Based on displacement experiments using site probes, viz., warfarin, ibuprofen and digitoxin, the site of binding of EMB in BSA was proposed to be Sudlow's site I. The effect of EMB on the conformation of BSA was analyzed by using synchronous fluorescence spectra (SFS) and 3D fluorescence spectra. The results of fluorescence, UV/vis absorption and FTIR spectra showed that the conformation of BSA was changed in the presence of EMB. The thermodynamic parameters including enthalpy change (ΔH0), entropy change (ΔS0) and free energy change (ΔG0) for BSA–EMB were calculated according to the van't Hoff equation and are discussed.
ISSN:1522-7235
1522-7243
DOI:10.1002/bio.3169