Part I: Surface-Enhanced Raman Spectroscopy Investigation of Amino Acids and Their Homodipeptides Adsorbed on Colloidal Silver

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Abstract:

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.

Keywords: AMINO ACIDS; HOMODIPEPTIDES; RAMAN SPECTROSCOPY; SERS; SILVER COLLOID; SURFACE-ENHANCED RAMAN SCATTERING

Document Type: Research Article

DOI: http://dx.doi.org/10.1366/000370204774103408

Affiliations: Laser Raman Laboratory, Regional Laboratory of Physicochemical Analysis and Structural Research, Jagiellonian University, 3Ingardena Street, 30-060 Krakow, Poland

Publication date: May 1, 2004

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