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Issue 22, 2014
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Conformational modulation of peptide secondary structures using β-aminobenzenesulfonic acid

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Abstract

This communication describes the influence of β-aminobenzenesulfonic acid (SAnt) on the conformational preferences of hetero foldamers. The designed (Aib-SAnt-Aib)n and (Aib-SAnt-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.

Graphical abstract: Conformational modulation of peptide secondary structures using β-aminobenzenesulfonic acid

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Publication details

The article was received on 20 Nov 2013, accepted on 24 Jan 2014 and first published on 24 Jan 2014


Article type: Communication
DOI: 10.1039/C3CC48850K
Citation: Chem. Commun., 2014,50, 2886-2888
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    Conformational modulation of peptide secondary structures using β-aminobenzenesulfonic acid

    S. S. Kale, S. M. Kunjir, R. L. Gawade, V. G. Puranik, P. R. Rajamohanan and G. J. Sanjayan, Chem. Commun., 2014, 50, 2886
    DOI: 10.1039/C3CC48850K

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