Abstract
In this study, the molecular interactions between pepsin and three pyrethroid insecticides, including fenvalerate, cyhalothrin and deltamethrin, were investigated by multi-spectroscopic and molecular docking methods under mimic physiological pH conditions. The results indicated that all of these insecticides could interact with pepsin to form insecticide-pepsin complexes. The binding constants, number of binding sites and thermodynamic parameters measured at different temperatures indicated that these three pyrethroid insecticides could spontaneously bind with pepsin mainly through electrostatic forces and hydrophobic interactions with one binding site. According to the theory of Föster's non-radioactive energy transfer, the distance (r) between pepsin and three pyrethroid insecticides were all found to be less than 7 nm, which implied that the energy transfer occurred between pepsin and these insecticides, leading to the quenching of pepsin fluorescence. Synchronous and three-dimensional fluorescence, CD spectra and molecular docking results indicated that all tested pyrethroid insecticides bound directly into the enzyme cavity site and the binding of insecticides into the cavity influenced the microenvironment of the pepsin activity site which resulted in the extension of peptide strands of pepsin with loss of α-helix structures.Copyright © 2016 John Wiley & Sons, Ltd.
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