期刊
CHEMBIOCHEM
卷 11, 期 8, 页码 1083-1092出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201000062
关键词
angiogenesis; integrin; peptides; RGD; urea
资金
- Ligue Nationale contre le Cancer
- Association de la Recherche sur le Cancer
- CAMPLP
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 a-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) receptor 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.
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