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Issue 10, 2014
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Polythiazole linkers as functional rigid connectors: a new RGD cyclopeptide with enhanced integrin selectivity

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Abstract

Polythiazole amino acids clasp linear peptides to generate cyclic derivatives, however, the resulting species are not merely stapled peptides but bear a complex heterocyclic moiety displaying its intrinsic set of interactions. As a proof of concept, a bisthiazole moiety has been grafted onto an RGD sequence to deliver a new cilengitide analogue with improved integrin selectivity and remarkable in vivo antiangiogenic activity.

Graphical abstract: Polythiazole linkers as functional rigid connectors: a new RGD cyclopeptide with enhanced integrin selectivity

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Article information


Submitted
22 Feb 2014
Accepted
22 May 2014
First published
23 May 2014

Chem. Sci., 2014,5, 3929-3935
Article type
Edge Article

Polythiazole linkers as functional rigid connectors: a new RGD cyclopeptide with enhanced integrin selectivity

J. Ruiz-Rodríguez, M. Miguel, S. Preciado, G. A. Acosta, J. Adan, A. Bidon-Chanal, F. J. Luque, F. Mitjans, R. Lavilla and F. Albericio, Chem. Sci., 2014, 5, 3929
DOI: 10.1039/C4SC00572D

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