Surface-enhanced Raman scattering spectra (SERS) were measured for various amino acids: L-methionine (Met), L-cysteine (Cys), Lglycine (Gly), L-leucine (Leu), L-phenylalanine (Phe), and L-proline (Pro) and their homodipeptides (Met-Met, Cys-Cys, Gly-Gly, LeuLeu, Phe-Phe, and Pro-Pro) in silver colloidal solutions. The geometry and orientation of the amino acids or dipeptides on the silver surface, and their specific interaction with the surface, were deducted by detailed spectral analysis of the SERS spectra. This analysis has allowed us to propose the particular surface geometry of amino acids or dipeptides and also implied that C-C bonds were almost parallel to the surface, as evidenced by the absence of marker bands in the skeletal C-C stretching region of the spectra. Additionally, using "time-dependent" SERS measurements we solved an existing controversy regarding the binding specificity of Gly-Gly on the silver surface.

We present a Raman and surface-enhanced Raman scattering (SERS) study of the following proteins containing S-S group(s): alpha chymotrypsin (alpha-CHT), insulin, lysozyme, oxytocin (OXT), Streptomyces subtilisin inhibitor (SSI), and trypsin inhibitor (STI). The SERS study is performed in order to understand the adsorption mechanism of the above-mentioned proteins on a colloidal silver surface. The SERS spectra presented here show bands associated mainly with aromatic amino acid vibrations. In addition, two distinct vibrations of the -C-S-S-C- fragment are observed in the Raman and SERS spectra, i.e., nu(SS) and nu(CS). The enhancement of the nu(SS) vibration in the SERS spectra yields evidence that the intact disulfide bridge(s) is (are) located near the silver surface. This finding is supported by the presence of the nu(CS) mode(s). The presence of nus(COO-) and nu(C-COO-) in the SERS spectra in the 1384-1399 cm(-1) and 909-939 cm(-1) regions, respectively, indicate that the negatively charged COO- groups (aspartic and glutamic acids) assist in the binding on the positively charged silver surface. The Raman amide I and III bands observed in the 1621-1633 and 1261-1289 cm(-1) ranges, respectively, indicate that the alpha-helical conformation is favored for binding to the surface over the random coil or beta-sheet conformations. In addition, the presence of the imino group of Trp and/or His indicates that these amino acid residues may also bind to the silver sol.

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.