Helical peptides from VEGF and Vammin hotspots for modulating the VEGF–VEGFR interaction
| Autor: | María Jesús Pérez de Vega, Nathalie Gagey-Eilstein, Nicolas Inguimbert, Marie Reille-Seroussi, Mercedes Martín-Martínez, Susana González-López, María Isabel García-Aranda, María Teresa García-López, Michel Vidal, María Angeles Jiménez, Clara M. Santiveri, Rosario González-Muñiz |
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| Rok vydání: | 2013 |
| Předmět: |
Models
Molecular Vascular Endothelial Growth Factor A Protein Conformation Protein-protein interactions Stereochemistry Angiogenesis VEGF receptors Peptide Viper Venoms Biochemistry Protein–protein interaction chemistry.chemical_compound Amide Physical and Theoretical Chemistry Receptor Nuclear Magnetic Resonance Biomolecular Helical structures chemistry.chemical_classification biology Chemistry Organic Chemistry VEGF Cyclic peptide Receptors Vascular Endothelial Growth Factor biology.protein Peptides |
| Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname |
| ISSN: | 1477-0539 1477-0520 |
| DOI: | 10.1039/c3ob27312a |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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