Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 47, Issue 1, Pages 60-67Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2010.03.020
Keywords
Human serum albumin; Methyl thiophanate; Fungicide; Fluorescence spectroscopy; Circular dichroism; SDS-PAGE
Funding
- Abdul Rahman Al-Jeraisy Chair for DNA Research, King Saud University, Riyadh, KSA
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Fluorescence quenching data on interaction of a fungicide methyl thiophanate (MT) with human serum albumin (HSA) elucidated a primary binding site at sub-domain IIA. Stern-Volmer algorithm and double log plot revealed the binding affinity (K-a) and capacity (n) of HSA as 1.65 x 10(4) M-1 and 1.0 (r(2)=0.99), respectively. Cyclic voltammetric and circular dichroism (CD) studies reaffirmed MT-HSA binding and demonstrated reduction in alpha-helical content of HSA. Substantial release of the carbonyl and acid-soluble amino groups from MT treated HSA suggested protein damage. The plausible mechanism of methyl (+CH3) group transfer from MT to side chain NH group of tryptophan and HSA degradation elucidates the toxicological and clinical implications of this fungicide. (C) 2010 Elsevier B.V. All rights reserved.
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