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Oligo( N ‐alkoxy glycines): Trans substantiating peptoid conformations
Author(s) -
Jordan Peter A.,
Paul Bishwajit,
Butterfoss Glenn L.,
Renfrew P. Douglas,
Bonneau Richard,
Kirshenbaum Kent
Publication year - 2011
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21675
Subject(s) - peptoid , chemistry , peptidomimetic , alkoxy group , amide , polyproline helix , combinatorial chemistry , reagent , stereochemistry , peptide bond , amino acid , organic chemistry , peptide , biochemistry , alkyl
Peptoid oligomers possess many desirable attributes as bioactive peptidomimetic agents, including their ease of synthesis, chemical diversity, and capability for molecular recognition. Ongoing efforts to develop functional peptoids will necessitate improved capability for control of peptoid structure, particularly of the backbone amide conformation. We introduce alkoxyamines as a new reagent for solid phase peptoid synthesis. Herein, we describe the synthesis of N ‐alkoxy peptoids, and present NMR data indicating that the oligomers adopt a single stable conformation featuring trans amide bonds. These findings, combined with results from computational modeling, suggest that N ‐alkoxy peptoid oligomers have a strong propensity to adopt a polyproline II type secondary structure. © 2011 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 96: 617–626, 2011.