Abstract
The adsorption of bovine serum albumin on silica of three different types, i.e., aerosil, macroporous silica gel, and ground natural quartz, was studied. The IR spectra of this protein adsorbed on aerosil were measured and analyzed. It was shown that the carbonyl groups of albumin macromolecules interact with vicinal hydroxyl groups while imido groups, with individual hydroxyl groups of silica surface. The geminal hydroxyl groups of the surface behaved as single adsorption sites with respect to albumin. The number or such sites on quartz surface was estimated. The IR spectra indicated that the adsorption of albumin macromolecules caused the dehydration of aerosil surface and the appearance of a small amount (to 10%) of unfolded β-regions in the secondary structure of the adsorbed protein, while the α-helical macromolecular structure remains preserved as a whole. Changes in the tertiary structure of the protein resulted from the adsorption were discussed. Protein macromolecules folded into globules were shown to be tilted with respect to the adsorbent surface.
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Tarasevich, Y.I., Monakhova, L.I. Interaction between Globular Proteins and Silica Surfaces. Colloid Journal 64, 482–487 (2002). https://doi.org/10.1023/A:1016828322434
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DOI: https://doi.org/10.1023/A:1016828322434