Abstract
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 × 10
5
−0.209 × 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 ΔG°, ΔH° and ΔS° 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.
Communicated by Ramaswamy H. Sarma