Conformational stability studies of a stapled hexa-β3-peptide library

Romila D. Gopalan; Mark P. Del Borgo; Ylva E. Bergman; Sharon Unabia; Roger J. Mulder; Matthew C. J. Wilce; Jacqueline A. Wilce; Marie-Isabel Aguilar; Patrick Perlmutter

doi:10.1039/C2OB06617C

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Conformational stability studies of a stapled hexa-β³-peptide library†‡

Romila D. Gopalan,§^ab Mark P. Del Borgo,§^b Ylva E. Bergman,^a Sharon Unabia,^b Roger J. Mulder,^c Matthew C. J. Wilce,^a Jacqueline A. Wilce,^b Marie-Isabel Aguilar*^b and Patrick Perlmutter*^a

Author affiliations

* Corresponding authors

^a School of Chemistry, Monash University, Clayton, VIC, Australia
E-mail: patrick.perlmutter@monash.edu
Fax: +613 9905 4597
Tel: +613 9905 4522

^b Department of Biochemistry & Molecular Biology, Monash University, Clayton, VIC, Australia
E-mail: mibel.aguilar@monash.edu
Fax: +613 9902 9500
Tel: +613 9905 3723

^c CSIRO, Clayton, VIC, Australia
E-mail: roger.mulder@csiro.au
Fax: +613 9545 2552
Tel: +613 9545 2550

Abstract

A library of 14-helical hexa β³-peptides was synthesized in order to determine the influence of sequence variation as well as staple size and location on conformational stability. From this study we show that appropriately stapled hexa-β³-peptides can allow for a number of variations without significant perturbation of the 14-helix.

This article is part of the themed collection: Foldamer Chemistry

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Article information

DOI: https://doi.org/10.1039/C2OB06617C
Article type: Paper
Submitted: 22 Sep 2011
Accepted: 06 Dec 2011
First published: 18 Jan 2012

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Org. Biomol. Chem., 2012,10, 1802-1806

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Conformational stability studies of a stapled hexa-β³-peptide library

R. D. Gopalan, M. P. Del Borgo, Y. E. Bergman, S. Unabia, R. J. Mulder, M. C. J. Wilce, J. A. Wilce, M. Aguilar and P. Perlmutter, Org. Biomol. Chem., 2012, 10, 1802 DOI: 10.1039/C2OB06617C

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Organic & Biomolecular Chemistry