(180g) Understanding the Cooperative Adsorption of Globular Proteins

Protein absorption on solid substrates has been studied extensively in regards to biofouling and biocompatibility of functional materials. However, the binding mechanism and cooperativity in protein adsorption onto functional surfaces are poorly understood. Here, the effect of solvent pH on the interactions between model proteins and silica materials is investigated. We found that both the electrostatic interaction and the protein molecular weight are markers of adsorption level and can be greater examined when exposed to a pH stimulus. From the adsorption isotherm studies, local hydrophobic interactions play a significant role on the binding of myoglobin on the silica surface local. The physical-chemical stability of myoglobin is brought into question at lower pH levels due to uncertain aggregation. This study lays a foundation for understanding complex bio-nano interactions and formation of protein corona onto nanoparticles.