Conformational modulation of peptide secondary structures using β-aminobenzenesulfonic acid

This communication describes the influence of β-aminobenzenesulfonic acid ((S)Ant) on the conformational preferences of hetero foldamers. The designed (Aib-(S)Ant-Aib)n and (Aib-(S)Ant-Pro)n oligomers display a well-defined folded conformation featuring intramolecular mixed hydrogen bonding (7/11) a...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2014-03, Vol.50 (22), p.2886-2888
Main Authors: Kale, Sangram S, Kunjir, Shrikant M, Gawade, Rupesh L, Puranik, Vedavati G, Rajamohanan, P R, Sanjayan, Gangadhar J
Format: Article
Language:English
Subjects:
Hydrogen Bonding
Modulation
Oligomers
Oligopeptides - chemistry
Peptides
Protein Structure, Secondary
Sulfanilic Acids - chemistry
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Summary:This communication describes the influence of β-aminobenzenesulfonic acid ((S)Ant) on the conformational preferences of hetero foldamers. The designed (Aib-(S)Ant-Aib)n and (Aib-(S)Ant-Pro)n oligomers display a well-defined folded conformation featuring intramolecular mixed hydrogen bonding (7/11) and intra-residual (6/5) H-bonding interactions, respectively.
ISSN:1359-7345
1364-548X
DOI:10.1039/c3cc48850k