Molecules | |
Design and Synthesis of C-Terminal Modified Cyclic Peptides as VEGFR1 Antagonists | |
Lei Wang1  Nathalie Gagey-Eilstein1  Sylvain Broussy1  Marie Reille-Seroussi1  Florent Huguenot1  Michel Vidal1  Wang-Qing Liu1  | |
[1] UMR 8638 CNRS, Faculté de Pharmacie de Paris, Université Paris Descartes, Sorbonne Paris Cité, 4 avenue de l’observatoire, Paris 75006, France; E-Mails: | |
关键词: VEGF; VEGFR; angiogenesis; cyclic peptides; | |
DOI : 10.3390/molecules191015391 | |
来源: mdpi | |
【 摘 要 】
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.
【 授权许可】
CC BY
© 2014 by the authors; licensee MDPI, Basel, Switzerland.
【 预 览 】
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