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 spectroscopy, 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 interaction 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.

Sodium dodecyl sulphate modulates the fibrillation of human serum albumin in a dose-dependent manner and impacts the PC12 cells retraction.

Protein aggregation is impacted by many factors including temperature, pH, and the presence of surfactants, electrolytes, and metal ions. The addition of sodium dodecyl sulphate (SDS) at different concentrations may play a significant role in the human serum albumin (HSA) fibrillation pathway. Here the heat induction of HSA fibrillation incubated with different concentrations of SDS was evaluated using a variety of techniques. These included ThT fluorescence, Congo red absorbance, circular dichroism, dynamic light scattering, and atomic force microscopy (AFM). To explore HSA surface properties, the surface tension of solutions was measured using Du Noüy Ring method tensiometry. In addition, the criteria of neurite outgrowth and complexity were monitored by exposing PC12 cells to different forms of HSA amyloid intermediates. ThT fluorescence kinetic studies indicated that SDS at low concentrations induced more fibrillation of HSA, while SDS at high concentrations inhibited the fibrillation of HSA. At higher SDS concentrations hydrophobic forces had a significant role whereas at lower SDS concentrations electrostatic forces were dominant. The cell culture studies demonstrated the significant impact of SDS concentration on HSA fibrillation and subsequent neuronal cell morphology. The HSA incubated with low concentrations of SDS inhibited neurite outgrowth and complexity of the PC12 cells, whereas high concentrations of SDS had lesser effect. Thus, SDS acts as a salt at lower concentrations, while at higher concentrations acts as a chaperon, with significant impact on fibrillation of HSA.