@article{555fb412e27b4b0c81f6b19778e341da,
title = "A {"}cross-stitched{"} peptide with improved helicity and proteolytic stability",
abstract = "A new computational approach to obtain quantitative energy profiles for helix folding was used in the design of orthogonal hydrocarbon and lactam bicyclic peptides. The proteolytically stable, {"}cross-stitched{"} peptide SRC2-BCP1 shows nanomolar affinity for estrogen receptor α and X-ray crystallography confirms a helical binding pose.",
author = "Speltz, {Thomas E.} and Mayne, {Christopher G.} and Fanning, {Sean W.} and Zamia Siddiqui and Emad Tajkhorshid and Greene, {Geoffrey L.} and Moore, {Terry W.}",
note = "Funding Information: This work was funded by the Chicago Biomedical Consortium with support from the Searle Funds at The Chicago Community Trust (to GLG and TWM), and in part by National Institutes of Health Grant P41-GM104601 (to ET). TES was funded by training grant T32AT007533, Office of the Director, National Institutes of Health and National Center for Complementary & Integrative Health. This work used XSEDE, supported by National Science Foundation grant number ACI-1548562, through allocations TG-MCA06N060 (to ET) and TG-MCB170062 (to TWM) with computing time on Bridges at the Pittsburgh Supercomputing Center and Stampede at the Texas Advanced Computing Center. Publisher Copyright: {\textcopyright} 2018 The Royal Society of Chemistry.",
year = "2018",
doi = "10.1039/c8ob00790j",
language = "English (US)",
volume = "16",
pages = "3702--3706",
journal = "Organic and Biomolecular Chemistry",
issn = "1477-0520",
publisher = "Royal Society of Chemistry",
number = "20",
}