Service interruption on Monday 11 July from 12:30 to 13:00: all the sites of the CCSD (HAL, EpiSciences, SciencesConf, AureHAL) will be inaccessible (network hardware connection).
Skip to Main content Skip to Navigation
Journal articles

Cyclization of peptides through a urea bond: application to the Arg-Gly-Asp tripeptide.

Abstract : Various synthetic cyclopeptides bind different cellular proteins with high affinity and specificity. In this study, we designed a new series of cyclic tetrapeptides containing the RGD sequence, a ligand for the alpha(v)beta(3) integrin receptor, in which the ring closure was performed through a urea bond between the alpha-amino group of the peptide and either the alpha- or the epsilon-amino group of an additional lysine. Interestingly, we showed that the urea-closed peptide had a higher affinity for alpha(v)beta(3) receptors than a reference pentacyclopeptide. Moreover, the synthetic strategy allows coupling of the resulting cyclic tetrapeptide through the carboxylic acid moiety of its lysine residue to fluorescent molecules or drugs. In addition, this strategy could be easily adapted for the cyclization of any other peptides.
Complete list of metadata
Contributor : Yves Le Ster Connect in order to contact the contributor
Submitted on : Tuesday, May 11, 2010 - 11:31:54 AM
Last modification on : Tuesday, July 5, 2022 - 8:53:19 AM
Long-term archiving on: : Thursday, December 1, 2016 - 1:00:30 AM


 Restricted access
To satisfy the distribution rights of the publisher, the document is embargoed until : jamais

Please log in to resquest access to the document

  •  ChemBioChem-VIVES2009revised2-.pdf    Embargoed until : jamais  Files produced by the author(s)



Julien Schmidt, Véronique Garambois, Luc Rocheblave, Jean Martinez, André Pèlegrin, et al.. Cyclization of peptides through a urea bond: application to the Arg-Gly-Asp tripeptide.. ChemBioChem, Wiley-VCH Verlag, 2010, 11 (8), pp.1083-92. ⟨10.1002/cbic.201000062⟩. ⟨inserm-00482710⟩



Record views