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

作者: Julien Schmidt , Véronique Garambois , Luc Rocheblave , Jean Martinez , André Pèlegrin

DOI: 10.1002/CBIC.201000062

关键词:

摘要: 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, ligand for alpha(v)beta(3) integrin receptor, in which ring closure was performed through urea bond between alpha-amino group peptide either alpha- or epsilon-amino an additional lysine. Interestingly, showed that urea-closed had higher receptors than reference pentacyclopeptide. Moreover, strategy allows coupling resulting tetrapeptide carboxylic acid moiety its lysine residue to fluorescent molecules drugs. addition, could be easily adapted cyclization any other peptides.

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