Local Surface Electric Field’s Effect on Adsorbed Proteins’ Orientation

Abstract

Hydrogenated nanocrystalline silicon, while being non-charged and non-polar, could be an ideal candidate for the non-covalent and orientation-controlled immobilization of biomolecules thanks to local electric fields around nanocrystals. To that effect, the adsorption of bovine serum albumin on substrates with different densities of nanocrystals, revealed by Raman spectroscopy and X-ray diffraction, was studied using infrared spectroscopy and atomic force microscopy. It was found that the protein–surface interactions followed different mechanisms depending on the nanostructure at the surface: hydrophobic on the non-crystalline part of the surface and electrostatic around the crystalline part. These electrostatic interactions were driven by the electric fields that arose at the junction between crystalline and amorphous structures. These electric fields were found to be strong enough to interact with the amide dipoles, thereby reorienting the adsorbed protein molecules on this part of the surface. Nevertheless, the adsorbed proteins were found to be denatured, which was due to the surface chemistry, and not affected by the nanostructure.