Molecular simulation of bovine beta-lactoglobulin adsorbed onto a positively charged solid surface.

To obtain detailed insight into the mechanism of beta-lactoglobulin (beta-Lg) adsorption to a stainless steel surface at acidic pH, the adsorption of positively charged beta-Lg to a positively charged surface (Au (100) surface with virtual positive charge) was simulated using classical molecular dynamics. The initial orientation and position of beta-Lg on the surface were determined using Monte Carlo simulation using the implicit water system. Molecular dynamics simulation with the explicit water system was conducted for a 5 ns simulation time to monitor beta-Lg adsorption. To investigate surface charge density effects on adsorption of beta-Lg, the positive charge number per Au atom on the (100) surface, C, was varied from 0 to +0.0250|e|. Stable adsorption occurred in MD simulations when C was equal to or less than +0.0200|e|. Among these surface Au charge conditions, no large difference was observed in the vertical separation distance between the surface and the protein's center of mass, and the orientation angle. This fact indicates that the main interactions contributing to the adsorption were van der Waals interactions. The protein domain contacting the surface was near Thr125, agreeing with previous experimental studies. Considering simulation results and those previous experimental studies suggests a detailed adsorption mechanism of beta-Lg at acidic pH: beta-Lg molecule is adsorbed initially with the specific part of 125-135th residues close to the surface by van der Waals interactions. Simultaneously or subsequently, side carboxylic groups of acidic amino acid residues near the surface in 125-135th residues dissociate, leading to firmer adsorption by attractive electrostatic residue-surface interaction.