| Abstract
| - Protein interactions with surfaces are key to understanding the behavior of implantable medical devices. The opticaltechnique of reflection anisotropy spectroscopy (RAS) has considerable potential for the study of interactions betweenimportant biological molecules and surfaces. This study used RAS to investigate the adsorption of S amino acids ontoAu(110) in a liquid environment under different conditions of potential and pH. Certain spectral features can beassociated with the Au(110), as reported previously, while other features are assigned to bonds between the aminoacids and the Au surface. The RA spectra are shown to be influenced by the structure of the amino acid, the solutionpH, and the applied electrode potential. This work has assigned the negative feature at 2.5 eV to the Au−thiolate,bond while the positive feature at 2.5 eV is assigned to the disulfide bond. The broad spectral feature at 3.5 eV isattributed to the Au−amino interaction, while the sharper feature at slightly higher energy is associated with theAu−carboxylate interaction. Sulfur-containing amino acids are frequently found on the outside of protein moleculesand could be used to anchor the protein to the surface.
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