Issue 22, 2014
From the journal:

Chemical Communications

Conformational modulation of peptide secondary structures using β-aminobenzenesulfonic acid†‡

Sangram S. Kale,a   Shrikant M. Kunjir,b   Rupesh L. Gawade,c   Vedavati G. Puranik,c   P. R. Rajamohananb  and  Gangadhar J. Sanjayan*a  

* Corresponding authors

a Division of Organic Chemistry, National Chemical Laboratory, Homi Bhabha Road, Pune 411 008, India
E-mail: gj.sanjayan@ncl.res.in
Web: http://nclwebapps.ncl.res.in/gjsanjayan/index.html

b Central NMR Facility, National Chemical Laboratory, India

c Center for Materials Characterization, National Chemical Laboratory, India

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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Article information

DOI
https://doi.org/10.1039/C3CC48850K
Article type
Communication
Submitted
20 Nov 2013
Accepted
24 Jan 2014
First published
24 Jan 2014

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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