The primary stage of adhesion during implant infection is dominated by interactions of the surface proteins of the bacteria with the substrate atoms. In the current work, molecular dynamics (MD) simulations have been utilized to investigate the mechanics of the associated adhesion forces of bacteria on different surfaces. The unfolding of these adhesion proteins is investigated in order to map these events to earlier experiments on bacterial de-adhesion (using single cell force spectroscopy) with real-life substrates (i.e., ultrahigh molecular weight polyethylene, hydroxyapatite, Ti alloy, and stainless steel). The adhesion of Staphylococcus aureus adhesin (i.e., SpA) is observed by altering their orientation on the silica substrate through MD simulations, followed by capturing unfolding events of three adhesins (SpA, ClfA, and SraP) of variable lengths possessing different secondary structures. The output long-range and short-range interaction forces and consequent visualization of changes in the secondary structure of protein segments are presented during the de-adhesion process. Simulation results are correlated with extracted short-range forces (using Poisson regression) from real-life bacterial de-adhesion experiments. Insights into such protein-substrate interactions may allow for engineering of biomaterials and designing of nonbiofouling surfaces.
Keywords: adhesins; bacteria; biomaterial surfaces; molecular dynamics; protein interaction.