CHARGE-TRANSFER CHROMATOGRAPHIC STUDY OF THE BINDING OF COMMERCIAL PESTICIDES TO VARIOUS ALBUMINS

The interaction of 28 commercial pesticides with human and bovine serum albumin as well as with egg albumin was studied by charge-transfer reversed-phase thin-layer chromatography and the relative strength of the interaction was calculated. Only one pesticide interacted with egg albumin whereas the majority of pesticides bound both to bovine and human serum albumins. Stepwise regression analysis proved that the hydrophobicity parameters of pesticides exert a significant impact on their capacity to bind to serum albumins. These findings support the hypothesis that the binding of pesticides to albumins may involve hydrophilic forces occurring between the corresponding apolar substructures of pesticides and amino acid side chains. No linear correlation was found between the capacities of human and bovine serum albumins to bind pesticides.