Authors contributed equally to this work.
Stabilisation of a short α-helical VIP fragment by side chain to side chain cyclisation: a comparison of common cyclisation motifs by circular dichroism
Article first published online: 27 MAY 2013
Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.
Journal of Peptide Science
Volume 19, Issue 7, pages 423–432, July 2013
How to Cite
Frankiewicz, L., Betti, C., Guillemyn, K., Tourwé, D., Jacquot, Y. and Ballet, S. (2013), Stabilisation of a short α-helical VIP fragment by side chain to side chain cyclisation: a comparison of common cyclisation motifs by circular dichroism. J. Peptide Sci., 19: 423–432. doi: 10.1002/psc.2515
- Issue published online: 10 JUN 2013
- Article first published online: 27 MAY 2013
- Manuscript Accepted: 8 APR 2013
- Manuscript Revised: 15 MAR 2013
- Manuscript Received: 12 FEB 2013
- Helix stabilisation;
- circular dichroism;
- cyclisation motifs;
- ring-closing metathesis;
- Huisgen cycloaddition
A model octapeptide segment derived from vasoactive intestinal peptide (VIP) was utilised to investigate the effect of several conventional cyclisation methods on the α-helical conformation in short peptide fragments. Three of the classical macrocyclisation techniques (i.e. lactamisation, ring-closing metathesis and Huisgen cycloaddition) were applied, and the conformations of the resulting cyclic peptides, as well as their linear precursors, were compared by CD analysis. The visibly higher folding propensity of the triazole-tethered peptide after azide-alkyne CuAAC macrocyclisation illustrates that the secondary structure of a short peptide fragment can differ significantly depending on the chemical strategy used to covalently cross-link side chain residues in a ‘helical’ fragment. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.