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Fluorescent bovine serum albumin interacting with the antitussive quencher dextromethorphan: a spectroscopic insight
Author(s) -
Durgannavar Amar K.,
Patgar Manjanath B.,
Nandibewoor Sharanappa T.,
Chimatadar Shivamurti A.
Publication year - 2016
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.3040
Subject(s) - bovine serum albumin , chemistry , fluorescence , circular dichroism , analytical chemistry (journal) , quenching (fluorescence) , binding constant , absorption spectroscopy , fluorescence spectroscopy , absorption (acoustics) , acceptor , spectroscopy , fourier transform infrared spectroscopy , crystallography , chromatography , binding site , materials science , biochemistry , physics , quantum mechanics , composite material , condensed matter physics
The interaction of dextromethorphan hydrobromide (DXM) with bovine serum albumin (BSA) is studied by using fluorescence spectra, UV–vis absorption, synchronous fluorescence spectra (SFS), 3D fluorescence spectra, Fourier transform infrared (FTIR) spectroscopy and circular dichroism under simulated physiological conditions. DXM effectively quenched the intrinsic fluorescence of BSA. Values of the binding constant, K A , are 7.159 × 10 3 , 9.398 × 10 3 and 16.101 × 10 3 L/mol; the number of binding sites, n , and the corresponding thermodynamic parameters ΔG °, ΔH ° and ΔS ° between DXM and BSA were calculated at different temperatures. The interaction between DXM and BSA occurs through dynamic quenching and the effect of DXM on the conformation of BSA was analyzed using SFS. The average binding distance, r , between the donor (BSA) and acceptor (DXM) was determined based on Förster's theory. The results of fluorescence spectra, UV–vis absorption spectra and SFS show that the secondary structure of the protein has been changed in the presence of DXM. Copyright © 2015 John Wiley & Sons, Ltd.