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Molecules 2014, 19(10), 15391-15407; doi:10.3390/molecules191015391

Design and Synthesis of C-Terminal Modified Cyclic Peptides as VEGFR1 Antagonists

1
UMR 8638 CNRS, Faculté de Pharmacie de Paris, Université Paris Descartes, Sorbonne Paris Cité, 4 avenue de l'observatoire, Paris 75006, France
2
UF Pharmacocinétique et pharmacochimie, hôpital Cochin, AP-HP, 27 rue du Faubourg Saint Jacques, Paris 75014, France
*
Authors to whom correspondence should be addressed.
Received: 7 August 2014 / Revised: 12 September 2014 / Accepted: 17 September 2014 / Published: 26 September 2014
(This article belongs to the Special Issue Design and Study of Kinase Inhibitors)
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Abstract

Previously designed cyclic peptide antagonist c[YYDEGLEE]-NH2 disrupts the interaction between vascular endothelial growth factor (VEGF) and its receptors (VEGFRs). It represents a promising tool in the fight against cancer and age-related macular degeneration. We described in this paper the optimization of the lead peptide by C-terminal modification. A new strategy for the synthesis of cyclic peptides is developed, improving the cyclisation efficiency. At 100 µM, several new peptides with an aromatic group flexibly linked at C-terminal end showed significantly increased receptor binding affinities in competition ELISA test. The most active peptide carrying a coumarin group may be a useful tool in anti-angiogenic biological studies. View Full-Text
Keywords: VEGF; VEGFR; angiogenesis; cyclic peptides VEGF; VEGFR; angiogenesis; cyclic peptides
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Wang, L.; Gagey-Eilstein, N.; Broussy, S.; Reille-Seroussi, M.; Huguenot, F.; Vidal, M.; Liu, W.-Q. Design and Synthesis of C-Terminal Modified Cyclic Peptides as VEGFR1 Antagonists. Molecules 2014, 19, 15391-15407.

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