Dresden 2006 – scientific programme

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O: Oberflächenphysik

O 14: Poster session I (Adsorption, Epitaxy and growth, Phase transitions, Surface reactions, Organic films, Electronic structure, Methods) (sponsored by Omicron Nanotechnology GmbH)

O 14.69: Poster

Monday, March 27, 2006, 18:00–21:00, P2

Innershell absorption spectroscopy of amino acids at all relevant absorption edges — •Yan Zubavichus^1,2, Andrey Shaporenko¹, Michael Grunze¹, and Michael Zharnikov¹ — ¹Angewandte Physikalische Chemie, Universität Heidelberg, INF 253, 69120, Heidelberg — ²Institute of Organoelement Compounds, Russian Academy of Sciences, 28 Vavilov st.,119991 Moscow, Russia

Application of X-ray absorption spectroscopy to bioorganic objects opens new possibilities for study of biologically-relevant processes at molecular level. However, such studies are difficult for various reasons, including the complexity of the molecular composition and radiation sensitivity of the target objects, so that the simplest of these objects, such as e.g. proteinogenic amino acids, which are building blocks of biological macromolecules, should be studied at first. Keeping this goal in mind, we acquired the C, N, and O K-edge near-edge X-ray absorption fine structure (NEXAFS) spectra of the 22 most common proteinogenic alpha-amino acids in the zwitter-ionic form. The spectra were collected from solvent-free polycrystalline powder films of the amino acids in the partial electron yield mode. Spectral features common to all amino acids, as well as distinctive fingerprints of specific subgroups of these compounds were identified and analyzed in detail. The obtained spectral library is an important step to establish such a powerful technique as NEXAFS spectroscopy to study complex systems of biological significance. This work was supported by BMBF (05 KS4VHA/4 and 05 KS4WWA/6) and the Russian Foundation for Basic Research (05-03-32871a).