These authors contributed equally to this work.
Rotaxane-Based Propeptides: Protection and Enzymatic Release of a Bioactive Pentapeptide†
Article first published online: 27 JUL 2009
Copyright © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 48, Issue 35, pages 6443–6447, August 17, 2009
How to Cite
Fernandes, A., Viterisi, A., Coutrot, F., Potok, S., Leigh, David A., Aucagne, V. and Papot, S. (2009), Rotaxane-Based Propeptides: Protection and Enzymatic Release of a Bioactive Pentapeptide. Angew. Chem. Int. Ed., 48: 6443–6447. doi: 10.1002/anie.200903215
We thank Prof. Jean-Pierre Gesson (Poitiers) for many useful discussions and the EPSRC National Mass Spectrometry Service Centre (Swansea, UK) for accurate mass data. This work was supported by the Science and Technology Department of the French Embassy in the United Kingdom, the Scottish Executive and the Royal Society of Edinburgh. D.A.L. is an EPSRC Senior Research Fellow and holds a Royal Society-Wolfson Research Merit Award.
- Issue published online: 12 AUG 2009
- Article first published online: 27 JUL 2009
- Manuscript Received: 14 JUN 2009
- Science and Technology Department of the French Embassy in the United Kingdom
- Scottish Executive and the Royal Society of Edinburgh
- delivery systems;
- supramolecular chemistry
Ring of protection: A rotaxane 1 protects and selectively releases a bioactive pentapeptide. The rotaxane macrocycle provides a defensive shield that very significantly improves the poor stability of the peptide to both individual peptidases and the cocktail of enzymes present in human plasma. Glycosidase-catalyzed cleavage of a carbohydrate ‘stopper’ in the rotaxane triggers release of the parent peptide (see picture).