Journal
JOURNAL OF ORGANIC CHEMISTRY
Volume 74, Issue 17, Pages 6703-6713Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jo901277a
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Funding
- Deutsche Forschungsgemeinschaft [2346/1-3, SFB 610]
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An (S)-C-linked carbo-e-amino acid [(S)-epsilon-Caa((x))] was prepared from the known (S)-delta-Caa. This monomer was utilized together With L-Ala to give novel alpha/epsilon-hybrid peptides in 1: 1 alternation. Conformational analysis on penta- and hexapeptides by NMR (in CDCl3), CD, and MD studies led to the identification of robust 14/12-mixed helices. This is in agreement with the data from a theoretical conformational analysis on the basis of ab initio MO theory providing a complete overview on all formally possible hydrogen-bonded helix patterns of alpha/epsilon-hybrid peptides with 1:1 backbone alternation, The new motif of a mixed 14/12-helix Was predicted as most stable in vacuum. Obviously, the formation of ordered secondary structures is also possible in peptide foldamers with amino acid constituents of considerable backbone lengths. Thus, alpha/epsilon-hybrid peptides expand the domain of foldamers and allow the introduction of desired functionalities via the alpha-amino acid constituents.
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