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 (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 ((+)CH(3)) group transfer from MT to side chain NH group of tryptophan and HSA degradation elucidates the toxicological and clinical implications of this fungicide.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Saquib Q,Al-Khedhairy AA,Alarifi SA,Dwivedi S,Mustafa J,Musarrat Jdoi
10.1016/j.ijbiomac.2010.03.020subject
Has Abstractpub_date
2010-07-01 00:00:00pages
60-7issue
1eissn
0141-8130issn
1879-0003pii
S0141-8130(10)00113-3journal_volume
47pub_type
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