Protein adsorption onto nanoparticle surfaces is a phenomenon that is crucial to understanding the behavior of nanoparticles in biological systems. In these studies, the interactions between a model protein, bovine serum albumin (BSA), two metal oxide nanoparticle surfaces (TiO2, 22 nm and SiO2, 14 nm) were studied at different pH values (pH 7.4, 4.5, and 2.0) and in the presence or absence of phosphate on the TiO2 surface. The results indicated that protein structure and protein surface coverage highly depend on both pH and nanoparticle type. At acidic pH, BSA completely denatured on the TiO2 surface and protein adsorption was a factor of three to ten times higher on TiO2 than on SiO2. The co-adsorption of phosphate to the TiO2 nanoparticle surface resulted in a decreased impact on the secondary structure of BSA, particularly at acidic pH where BSA only denatured in the absence of co-adsorbed phosphate. Taken together, this information provides a systematic understanding of how the secondary protein structure can be altered as a function of nanoparticle surface chemistry, solution pH, and co-adsorbed oxyanions.

Bovine serum albumin adsorption on metal oxide nanoparticles: Effects of pH, nanoparticle surface, and co-adsorbed oxyanions on protein-surface interactions and protein structure

254th National Meeting (2017)

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