BSA adsorption onto nanospheres: Influence of surface curvature as probed by electrophoretic light scattering and UV/vis spectroscopy

作者：Sanchez Perez Julio A; Gallardo Moreno Amparo M; Luisa Gonzalez Martin M; Vadillo Rodriguez Virginia^*

来源：Applied Surface Science, 2015, 353: 1095-1102.

DOI：10.1016/j.apsusc.2015.06.198

• BSA
• Protein adsorption
• Surface curvature
• Nanospheres
• Zeta potential
• Adsorption isotherms

The influence of surface curvature on the adsorption of bovine serum albumin (BSA) was evaluated through the combination of two fairly simple techniques: electrophoretic light scattering and UV/vis spectroscopy. Measurements were carried out for a range of protein concentrations (0-320 mu g/ml) at pH 3.5, 4.5 and 7 using hydrophobic polystyrene nano spheres of 38.8, 82 and 220 nm in diameter. The results obtained demonstrate that the charge of the BSA molecules in solution dictates the pH-dependent behavior of the protein-coated nanospheres, indicating in all cases a significant adsorption of BSA molecules. At a fixed pH, however, it is the zeta potential that characterizes the uncoated nanospheres normalized by their surface area that primarily controls protein adsorption. In particular, it is found that the rate at which BSA interact with the different nanospheres increases as their negative zeta potential per unit area (or diameter) increases (decreases) regardless of the pH. Moreover, provided that adsorption occurs away from the isoelectric point of the protein, highly curved surfaces are found to stabilize the native-like conformation of BSA upon adsorption by likely reducing lateral interactions between adsorbed molecules.

• 出版日期2015-10-30