Design and Synthesis of C-Terminal Modified Cyclic Peptides as VEGFR1 Antagonists
AbstractPreviously 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
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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.
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(10):15391-15407.Chicago/Turabian Style
Wang, Lei; Gagey-Eilstein, Nathalie; Broussy, Sylvain; Reille-Seroussi, Marie; Huguenot, Florent; Vidal, Michel; Liu, Wang-Qing. 2014. "Design and Synthesis of C-Terminal Modified Cyclic Peptides as VEGFR1 Antagonists." Molecules 19, no. 10: 15391-15407.