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Título: | Helical peptides from VEGF and Vammin hotspots for modulating the VEGF-VEGFR interaction |
Autor: | García-Aranda, M. Isabel CSIC; González-López, Susana CSIC; Santiveri, Clara M. CSIC ORCID; Gagey-Eilstein, Nathalie; Reille-Seroussi, Marie; Martín-Martínez, Mercedes CSIC ORCID; Inguimbert, Nicolas; Vidal, Michel; García-López, M. Teresa CSIC ; Jiménez, M. Angeles CSIC ORCID ; González-Muñiz, Rosario CSIC ORCID; Pérez de Vega, M. Jesús CSIC ORCID | Palabras clave: | VEGF Peptides Helical structures Protein-protein interactions Angiogenesis |
Fecha de publicación: | 2013 | Editor: | Royal Society of Chemistry (UK) | Citación: | Organic and Biomolecular Chemistry 11: 1896-1905 (2013) | Resumen: | 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 algorithm and prepared following peptide solid-phase synthetic protocols. Cyclic peptide derivatives were prepared on-resin from linear precursors with conveniently located Glu and Lys residues, by the formation of amide linkages. Conformational analysis, CD and NMR, showed that most synthesized peptides have a clear tendency to be structured as α-helices in solution. Some of the peptides were able to bind a VEGFR-1 receptor with moderate affinity. In addition to the described key residues (Phe17, Tyr21 and Tyr25), Val14 and Val20 seem to be relevant for affinity. | URI: | http://hdl.handle.net/10261/103196 | DOI: | 10.1039/c3ob27312a | Identificadores: | doi: 10.1039/c3ob27312a issn: 1477-0520 e-issn: 1477-0539 |
Aparece en las colecciones: | (IQM) Artículos (IQF) Artículos |
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Org. Biomol. Chem., 2013, 11,.pdf | 1,74 MB | Adobe PDF | Visualizar/Abrir |
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