Issue 16, 2008
From the journal:

Organic & Biomolecular Chemistry

Stable helical peptoids via covalent side chain to side chain cyclization†

Belén Vaza  and  Luc Brunsveld*a  

* Corresponding authors

a Max Planck Institute of Molecular Physiology, Otto-Hahn Straße 11, and Chemical Genomics Centre, Otto-Hahn Straße 15, Dortmund, Germany
E-mail: luc.brunsveld@mpi-dortmund.mpg.de
Fax: +49 231 1332499
Tel: +49 231 97426473

Abstract

Peptoids are oligomeric N-substituted glycines with potential as biologically relevant compounds. Helical peptoids provide an attractive fold for the generation of protein–protein interaction inhibitors. The generation of helical peptoid folds in organic and aqueous media has been limited to strict design rules, as peptoid-folding is mainly directed via the steric direction of α-chiral side-chains. Here a new methodology is presented to induce helical folds in peptoids with the aid of side chain to side chain cyclization. Cyclic peptoids were generated via solid-phase synthesis and their folding was studied. The cyclization induces significant helicity in peptoids in organic media, aids the folding in aqueous media, and requires the incorporation of only relatively few chiral aromatic side chains.

Graphical abstract: Stable helical peptoids via covalent side chain to side chain cyclization

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Article information

DOI
https://doi.org/10.1039/B806847J
Article type
Paper
Submitted
23 Apr 2008
Accepted
04 Jun 2008
First published
26 Jun 2008

Org. Biomol. Chem., 2008,6, 2988-2994

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Stable helical peptoids via covalent side chain to side chain cyclization

B. Vaz and L. Brunsveld, Org. Biomol. Chem., 2008, 6, 2988 DOI: 10.1039/B806847J

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