Probing the Binding Mechanism of Peptides on a Copper Surface: Multi layer Self-Assembly Promoted by Glutamate Residues

Short peptides interact strongly with copper surfaces We report here a full characterization on the Interaction of Gly-Pto and the Cu(110) surface: By combining infrared analysis with X-ray photoelectron spectroscopy, two binding centers have been identified: the carboxylate and the amino groups Moreover, spectral were used in an innovative way to evaluate the number of nitrogen atoms per molecule bound to the surface. The presence of additional glutamate fragment in the peptide modifies the adsorption mechanism radically, leading to multilayer self-assembling growth. Our findings open up new insights into interfacial phenomena involved in intermolecular bonds and molecule-surface interactions.