期刊
SURFACE SCIENCE
卷 600, 期 2, 页码 409-416出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.susc.2005.10.040
关键词
chemisorption; helical conformation; peptides; scanning tunneling microscopy; self-assembly; surface structure and topography
A novel hexapeptide was functionalized at the N-terminus by a lipoyl group for binding to gold substrates. Owing to the high content of alpha-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. (c) 2005 Elsevier B.V. All rights reserved.
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