Spectroscopic and molecular modelling study of binding mechanism of bovine serum albumin with phosmet.

Phosmet exerts its neurotoxicity by inhibiting acetylcholinesterase that catalyzes the degradation of acetylcholine (a neurotransmitter). Serum proteins are known to influence the biodistribution of various endogenous and exogenous compounds. In the present study, the binding interactions of phosmet with bovine serum albumin (BSA) was investigated to determine the free concentration of phosmet for its neurotoxicity. The binding mechanism was studied using fluorescence, UV-Vis absorption spectroscopy, circular dichroism (CD), and molecular docking techniques. UV-Vis absorption data showed an increase in absorbance of BSA upon binding with phosmet with a slight red-shift in the peak around 280 nm. Intrinsic fluorescence of BSA was quenched in the presence of phosmet. The quenching was observed to be inversely correlated to the temperature that indicated the formation of ground state non-fluorescent complex (static quenching). Binding constant values and n values for the binding of phosmet with BSA at three different temperatures confirmed non-covalent binding interactions with a single set of equivalent binding sites. Thermodynamic parameters ∆G (-137.40 ± 3.58 kJ mol

Informations de copyright

Copyright © 2020 Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest There is no conflict of interest among the authors.