Part I: Surface-Enhanced Raman Spectroscopy Investigation of Amino Acids and Their Homodipeptides Adsorbed on Colloidal Silver
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.
Document Type: Research Article
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
More about this publication?
- The Society publishes the internationally recognized, peer reviewed journal, Applied Spectroscopy, which is available both in print and online. Subscriptions are included with membership or can be purchased by institutional or corporate organizations. Abstracts may be viewed free of charge. Previously published as Bulletin (Society for Applied Spectroscopy)
- Editorial Board
- Information for Authors
- Submit a Paper
- Subscribe to this Title
- Membership Information
- Request copyrighted SAS materials
- Spectroscopic Nomenclature
- Focal Point (Open Access)
- ingentaconnect is not responsible for the content or availability of external websites