A novel hexapeptide was functionalized at the N-terminus by a lipoyl group for binding to gold substrates. Owing to the high content of α-aminoisobutyric acid residues, the peptide adopts a rigid helical conformation despite the shortness of its main chain. Binding of the peptide to gold was investigated by quartz crystal microbalance, cyclic voltammetry, X-ray photoelectron spectroscopy, and scanning tunneling microscopy under ultra-high vacuum conditions. Scanning tunneling microscopy experiments revealed that the peculiar self-assembly properties of this short helical peptide determine the complex morphology of the monolayer, showing ‘stripes’, i.e. peptide aggregates horizontally layered on the gold surface, and ‘holes’, i.e. Au vacancy islands coated by the peptide monolayer.
15 Jan 2006
Volume: 600 Issue: 2 Pages: 409-416