@article{b55ac9ab20a64e609fe774282bee79fc,
title = "Peptide-functionalized semiconductor surfaces: Strong surface electronic effects from minor alterations to backbone composition",
abstract = "The use of non-canonical amino acids is a powerful way to control protein structure. Here, we show that subtle changes to backbone composition affect the ability of a dipeptide to modify solid surface electronic properties. The extreme sensitivity of the interactions to the peptide structure suggests potential applications in improving the performance of electronic devices.",
author = "Maayan Matmor and Lengyel, {George A.} and Horne, {W. Seth} and Nurit Ashkenasy",
note = "Funding Information: This research was supported by the Israel Science Foundation (grant no. 1519/14). We thank Dr S. Kolusheva from the Ilse Katz Institute for Nanoscale Science and Technology (IKI, Ben Gurion University) and Prof. D. Cahen and Ms S. Raichlin (Weizmann Institute of Science) for their assistance with the FTIR measurements and their interpretation. M. M. is a recipient of a Kreitman PhD fellowship. Publisher Copyright: {\textcopyright} 2017 the Owner Societies.",
year = "2017",
month = jan,
day = "1",
doi = "10.1039/c6cp07198h",
language = "English",
volume = "19",
pages = "5709--5714",
journal = "Physical Chemistry Chemical Physics",
issn = "1463-9076",
publisher = "Royal Society of Chemistry",
number = "8",
}