Podstawka Edyta, Ozaki Yukihiro, Proniewicz Leonard M
Laser Raman Laboratory, Regional Laboratory of Physicochemical Analysis and Structural Research, Jagiellonian University, ul. Ingardena 3, 30-060 Krakow, Poland.
Appl Spectrosc. 2005 Dec;59(12):1516-26. doi: 10.1366/000370205775142520.
Surface-enhanced Raman scattering (SERS) spectra were measured for monolayers of various amino acids: L-methionine (Met), L-cysteine (Cys), L-glycine (Gly), L-leucine (Leu), L-phenylalanine (Phe), and L-proline (Pro) and their homodipeptides (Met-Met, Cys-Cys, Gly-Gly, Leu-Leu, Phe-Phe, and Pro-Pro) deposited onto a colloidal gold surface. Orientation of amino acids and their homodipeptides, as well as specific-competitive interactions of their functional groups with the gold surface, were predicted by detailed spectral analysis of the obtained SERS spectra. The analysis performed allowed us to propose a particular surface geometry for each amino acid and homodipeptide on the gold surface. In addition, we compared the structures of these molecules adsorbed on colloidal gold and silver surfaces.
测量了各种氨基酸（L-甲硫氨酸（Met）、L-半胱氨酸（Cys）、L-甘氨酸（Gly）、L-亮氨酸（Leu）、L-苯丙氨酸（Phe）和L-脯氨酸（Pro））及其同型二肽（Met-Met、Cys-Cys、Gly-Gly、Leu-Leu、Phe-Phe和Pro-Pro）单层沉积在胶体金表面的表面增强拉曼散射（SERS）光谱。通过对所得SERS光谱的详细光谱分析，预测了氨基酸及其同型二肽的取向，以及它们的官能团与金表面的特异性竞争相互作用。所进行的分析使我们能够为金表面上的每种氨基酸和同型二肽提出特定的表面几何结构。此外，我们比较了吸附在胶体金和银表面的这些分子的结构。
Zotero 插件