Issue 2, 2009
From the journal:

Chemical Communications

Sculpting the β-peptide foldamer H12 helix via a designed side-chain shape†

Anasztázia Hetényi,a   Zsolt Szakonyi,a   István M. Mándity,a   Éva Szolnoki,a   Gábor K. Tóth,b   Tamás A. Martinek*a  and  Ferenc Fülöp*a  

* Corresponding authors

a Institute of Pharmaceutical Chemistry, University of Szeged, Szeged, Hungary
E-mail: martinek@pharm.u-szeged.hu, fulop@pharm.u-szeged.hu
Fax: (+36) 62-545705
Tel: (+36) 62-545768

b Department of Medical Chemistry, University of Szeged, Szeged, Hungary

Abstract

The long-range side-chain repulsion between the (1R,2R,3R,5R)-2-amino-6,6-dimethyl-bicyclo[3.1.1]-heptane-3-carboxylic acid (trans-ABHC) residues stabilize the H12 helix in β-peptide oligomers.

Graphical abstract: Sculpting the β-peptide foldamer H12 helix via a designed side-chain shape

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Article information

DOI
https://doi.org/10.1039/B812114A
Article type
Communication
Submitted
15 Jul 2008
Accepted
23 Oct 2008
First published
14 Nov 2008

Chem. Commun., 2009, 177-179

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Sculpting the β-peptide foldamer H12 helix via a designed side-chain shape

A. Hetényi, Z. Szakonyi, I. M. Mándity, É. Szolnoki, G. K. Tóth, T. A. Martinek and F. Fülöp, Chem. Commun., 2009, 177 DOI: 10.1039/B812114A

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