Reflection anisotropy spectroscopy study of the adsorption of sulfur-containing amino acids at the Au(110)/electrolyte interface
Reflection anisotropy spectroscopy study of the adsorption of sulfur-containing amino acids at the Au(110)/electrolyte interface
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DOI：
10.1021/la052584u
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发表时间：
2006-03-28
期刊：
影响因子：
3.9
通讯作者：
Weightman, P
中科院分区：
文献类型：
--
作者：
LeParc, R;Smith, CI;Weightman, P
蛋白质与表面的相互作用是理解植入式医疗设备行为的关键。反射各向异性光谱(RAS)光学技术在研究重要生物分子与表面之间的相互作用方面具有很大的潜力。研究了在不同电位和pH条件下，液体环境中S氨基酸在Au(110)表面的吸附行为。如前所述，某些光谱特征可以与Au(110)相关联，而另一些特征则被指定为氨基酸和Au表面之间的键。结果表明，氨基酸的结构、溶液的pH和外加的电极电位都会影响RA光谱。这项工作将2.5 eV处的负特征归属于金硫键，而将2.5 eV处的正特征归属于二硫键。在3.5 eV处的宽谱特征归因于Au-氨基相互作用，而在稍高能量下的较尖锐特征与Au-羧酸盐相互作用有关。含硫氨基酸通常存在于蛋白质分子的外部，可以用来将蛋白质固定在表面。
Protein interactions with surfaces are key to understanding the behavior of implantable medical devices. The optical technique of reflection anisotropy spectroscopy (RAS) has considerable potential for the study of interactions between important biological molecules and Surfaces. This study used RAS to investigate the adsorption of S amino acids onto Au(110) in a liquid environment under different conditions of potential and pH. Certain spectral features can be associated with the Au(110), as reported previously, while other features are assigned to bonds between the amino acids and the Au Surface. The RA spectra are shown to be influenced by the structure of the amino acid, the solution pH, 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 is attributed to the Au-amino interaction, while the sharper feature at slightly higher energy is associated with the Au-carboxylate interaction. Sulfur-containing amino acids are frequently found on the outside of protein molecules and could be used to anchor the protein to the surface.