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Synthesis and Secondary Structure of Alternate α,β‐Hybrid Peptides Containing Oxazolidin‐2‐one Moieties
Author(s) -
Angelici Gaetano,
Luppi Gianlugi,
Kaptein Bernard,
Broxterman Quirinus B.,
Hofmann HansJörg,
Tomasini Claudia
Publication year - 2007
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.200700134
Subject(s) - chemistry , steric effects , stereochemistry , sequence (biology) , ab initio , nuclear magnetic resonance spectroscopy , protein secondary structure , helix (gastropod) , hydrogen bond , crystallography , molecule , organic chemistry , biology , ecology , biochemistry , snail
The synthesis and conformational analysis of a novel class of foldamers containing ( S )‐β 3 ‐homophenylglycine [( S )‐β 3 ‐hPhg] and D ‐4‐carboxy‐oxazolidin‐2‐one ( D ‐Oxd) residues in alternate order is reported. The experimental conformational analysis performed in solution by IR, 1 H NMR, and CD spectroscopy unambiguously proved that these oligomers fold into ordered structures with increasing sequence length. Theoretical calculations employing ab initio MO theory suggest a helix with 11‐membered hydrogen‐bonded rings as the preferred secondary structure type. The few formal helix alternatives can be excluded in particular by steric effects of the oxazolidin‐2‐one rings. The novel structures enrich the field of peptidic foldamers and might be useful in the mimicry of native peptides. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2007)