The role of surface activity on the amyloid fibrillation pathway of bovine serum albumin upon interaction with glyphosate

As an active ingredient in its derivative products, glyphosate has emerged as the most widespread herbicide in recent decades. Bovine serum albumin (BSA) as a carrier protein may be adversely affected by structural changes due to binding affinity with glyphosate, which may lead to dysfunctionality or metabolic disorders. This study aimed to investigate the interaction of glyphosate with BSA and its thermal fibrillation pathway employing techniques such as dynamic surface tension, fluorescence quenching, ThT binding, circular dichroism spec-troscopy, and reactive oxygen species (ROS) measurement, as well as molecular dynamics (MD) studies. The adsorption dynamic analysis suggested hydrophobic moiety at higher concentrations of glyphosate upon inter-action with BSA. MD results suggested a slight fluctuation due to glyphosate interaction with protein molecules. The carboxy group presented in glyphosate made a hydrogen bond with the hydroxyl group of TYR147. The fluorescence quenching and diffusion studies approved BSA's increased unfolding and hydrophobicity resulting from glyphosate interaction, which would induce fibrillation/aggregation, according to our fibrillation kinetics data. The surface activity of glyphosate at higher concentrations and its approved involvement in structural changes of BSA through hydrogen bonding may raise concerns about its potential side effect on farm animals and the food cycle.

Automated summary

This study investigated the interaction of glyphosate with BSA and its thermal fibrillation pathway using various techniques. The results indicated that glyphosate interaction with BSA can cause structural changes, which may lead to dysfunctionality or metabolic disorders.