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

Autor: Luc Rocheblave, Jean Martinez, Eric Vivès, Julien Schmidt, Florine Cavelier, André Pèlegrin, Véronique Garambois
Přispěvatelé: Institut de recherche en cancérologie de Montpellier (IRCM - U896 Inserm - UM1), Université Montpellier 1 (UM1)-CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Le Ster, Yves, Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)
Jazyk: angličtina
Rok vydání: 2010
Předmět:
Lung Neoplasms
Lysine
Peptide
Angiogenesis Inhibitors
Tripeptide
Biochemistry
Mice
angiogenesis
0302 clinical medicine
Moiety
MESH: Animals
MESH: Cyclization
Receptor
Melanoma
MESH: Angiogenesis Inhibitors
chemistry.chemical_classification
0303 health sciences
RGD
[SDV.SP]Life Sciences [q-bio]/Pharmaceutical sciences
Ligand (biochemistry)
[SDV.SP] Life Sciences [q-bio]/Pharmaceutical sciences
MESH: Integrin alphaVbeta3
030220 oncology & carcinogenesis
MESH: Oligopeptides
Molecular Medicine
Oligopeptides
MESH: Cell Line
Tumor
Stereochemistry
integrin
MESH: Melanoma
Carboxylic acid
[SDV.CAN]Life Sciences [q-bio]/Cancer
urea
Cell Line
03 medical and health sciences
cyclopeptide
[SDV.CAN] Life Sciences [q-bio]/Cancer
MESH: Mice
Inbred C57BL
Cell Line
Tumor
[SDV.BBM] Life Sciences [q-bio]/Biochemistry
Molecular Biology
Animals
Humans
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
Molecular Biology
MESH: Mice
MESH: Urea
030304 developmental biology
MESH: Humans
Tetrapeptide
Organic Chemistry
Integrin alphaVbeta3
Combinatorial chemistry
MESH: Cell Line
MESH: Lung Neoplasms
Mice
Inbred C57BL
chemistry
Cyclization
Zdroj: ChemBioChem
ChemBioChem, 2010, 11 (8), pp.1083-92. ⟨10.1002/cbic.201000062⟩
ChemBioChem, Wiley-VCH Verlag, 2010, 11 (8), pp.1083-92. ⟨10.1002/cbic.201000062⟩
ISSN: 1439-4227
1439-7633
DOI: 10.1002/cbic.201000062⟩
Popis: International audience; 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.
Databáze: OpenAIRE
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