Insights into the interaction of azinphos-methyl with bovine serum albumin: experimental and molecular docking studies

In the present study, combining spectroscopic and molecular modeling techniques has been used to analyze azinphos-methyl binding properties, as an organophosphorus pesticide, to bovine serum albumin. The quenching interaction of azinphos-methyl with bovine serum albumin was investigated in an appropriate physiological state (pH = 7.4). Fluorescence spectroscopy, UV-visible spectroscopy, circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR). Findings showed differences in the secondary protein structure microenvironment following interaction with azinphos-methyl. The results from spectroscopic experiments suggest that azinphos-methyl binds to bovine serum albumin residues with a binding constant in the range of 0.099 x 10(5) 0.209 x 10(5) M-1 in one binding site (Tyr 160). The experimental results are supported by computational techniques such as docking using a bovine serum albumin crystal model. The results show that azinphos-methyl is linked to the site I of bovine serum albumin (in subdomain IB), and the result was in accordance with the experimental result. Based on the negative Delta G degrees, Delta H degrees and Delta S degrees values, the binding between azinphos-methyl and bovine serum albumin was spontaneous, and docking studies confirmed hydrogen bonding and van der Waals forces between them.

Automated summary

In this study, spectroscopic and molecular modeling techniques were used to analyze the binding properties of azinphos-methyl, an organophosphorus pesticide, to bovine serum albumin. The results showed changes in the secondary protein structure microenvironment following the interaction between azinphos-methyl and bovine serum albumin. Spectroscopic experiments indicated that azinphos-methyl bound to bovine serum albumin residues with a binding constant in a specific range, providing insights into the binding mechanism.