Surface Effects on Both Protein Structure and Solvation by the Atrftir Technique

We investigate protein adsorption on three types of planar solid supports, classified as hydrophilic or hydrophobic model surfaces. The planar model supports are obtained by modifying the native silica surface of the ATR crystal with «-functionalised alkylsilanes bearing a bromo or a methyl group at the end. The chemical transformation of the bromo-terminated SAMs enables the production of a polar aminated support (Noinville et al. 2003). Among the two hydrophilic supports, the native silica surface of the ATR crystal is used as a negatively charged surface, while the ND2-terminated SAMs, still not protonated at pD 7.5, is considered as a neutral support. We will present infrared results performed with hydrosoluble proteins such as BSA and lysozyme chosen as illustrative cases of adsorption of respectively soft and hard proteins on the three different types of supports. Then we will present results that clarify the role of the protein nature and size specifically during adsorption onto hydrophobic supports.

Before reviewing the results concerning the surface-induced conforma-tional changes, we introduce the specific processing of infrared spectra of proteins.

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