Helical peptides from VEGF and Vammin hotspots for modulating the VEGF-VEGFR interaction

The design, synthesis, conformational studies and binding affinity for VEGF receptors of a collection of linear and cyclic peptide analogues of the N-terminal α-helix fragments 13-25 of VEGF and 1-13 of Vammin are described. Linear 13(14)-mer peptides were designed with the help of an AGADIR algorit...

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Veröffentlicht in:	Organic & biomolecular chemistry 2013-03, Vol.11 (11), p.1896-1905
Hauptverfasser:	García-Aranda, María Isabel, González-López, Susana, Santiveri, Clara María, Gagey-Eilstein, Nathalie, Reille-Seroussi, Marie, Martín-Martínez, Mercedes, Inguimbert, Nicolas, Vidal, Michel, García-López, María Teresa, Jiménez, María Angeles, González-Muñiz, Rosario, Pérez de Vega, María Jesús
Format:	Artikel
Sprache:	eng
Schlagworte:	Models, Molecular Nuclear Magnetic Resonance, Biomolecular Peptides - chemical synthesis Peptides - chemistry Peptides - metabolism Protein Conformation Receptors, Vascular Endothelial Growth Factor - chemistry Receptors, Vascular Endothelial Growth Factor - metabolism Vascular Endothelial Growth Factor A - chemistry Viper Venoms - chemistry
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