Regensburg 2013 – wissenschaftliches Programm
O 42.3: Vortrag
Mittwoch, 13. März 2013, 11:00–11:15, H38
The molecular structure of a nine amino acid peptide at metal surfaces in vacuum — •Gordon Rinke1, Stephan Rauschenbach1, Rico Gutzler1, Alyazan Albargash1, Ludger Hanau2, and Klaus Kern1,3 — 1Max-Planck Institute for Solid State Research, Stuttgart, Germany — 2Max-Planck Institute for Intelligent Systems, Stuttgart, Germany — 3Institut de Physique de la Matiere Condensee, EPF Lausanne, Switzerland
Self-assembly of small molecules at surfaces in ultrahigh vacuum (UHV) is typically described as the interplay of intermolecular and molecule-surface interactions. Significant conformational changes or intramolecular interactions are rarely considered in this picture of self-assembly because these are relevant only for large molecules, which cannot be brought to surfaces in UHV by conventional deposition methods. The combination of electrospray ion beam deposition and scanning tunneling microscopy (STM) allowed us to study the molecular self-assembly of proteins and peptides in UHV.
In this study we address the self-assembly of Bradykinin (BK), a nine amino acid peptide with a mass of 1060u and large enough to interact with itself. Experimentally we find several conformations of BK in single molecule and dimer structures as well as in a superstructure of dimers. Conformations suggested by molecular dynamics simulations and calculated by density functional theory are compared to STM topographies and provide a tentative model of the adsorption.
Our study suggests that rationally synthesized peptides on surfaces can fold into structures with unique catalytic and chemical functions.