Fungicide methyl thiophanate binding at sub-domain IIA of human serum albumin triggers conformational change and protein damage

Journal Article
J, Saquib, Q., Al-Khedhairy, A.A., Al-Arifi, S., Dwivedi, S., Mustafa, J., Musarrat, . 2010
Publication Work Type: 
KSU Research Work
Magazine \ Newspaper: 
International Journal of Biological Macromolecules
Issue Number: 
1
Volume Number: 
47
Pages: 
60–67
Publication Abstract: 

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 (Ka) and capacity (n) of HSA as 1.65 × 104 M−1 and 1.0 (r2 = 0.99), respectively. Cyclic voltammetric and circular dichroism (CD) studies reaffirmed MT–HSA binding and demonstrated reduction in α-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.