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- W2037751555 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." @default.
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- W2037751555 date "2010-07-01" @default.
- W2037751555 modified "2023-09-29" @default.
- W2037751555 title "Fungicide methyl thiophanate binding at sub-domain IIA of human serum albumin triggers conformational change and protein damage" @default.
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- W2037751555 doi "https://doi.org/10.1016/j.ijbiomac.2010.03.020" @default.
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