English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/103196
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

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

AuthorsGarcía-Aranda, M. Isabel ; González-López, Susana; Santiveri, Clara M.; Gagey-Eilstein, Nathalie; Reille-Seroussi, Marie; Martín-Martínez, Mercedes ; Inguimbert, Nicolas; Vidal, Michel; García-López, M. Teresa ; Jiménez, M. Angeles ; González-Muñiz, Rosario ; Pérez de Vega, M. Jesús
Helical structures
Protein-protein interactions
Issue Date2013
PublisherRoyal Society of Chemistry (UK)
CitationOrganic and Biomolecular Chemistry 11: 1896-1905 (2013)
AbstractThe 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.
Identifiersdoi: 10.1039/c3ob27312a
issn: 1477-0520
e-issn: 1477-0539
Appears in Collections:(IQM) Artículos
(IQFR) Artículos
Files in This Item:
File Description SizeFormat 
Org. Biomol. Chem., 2013, 11,.pdf1,74 MBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.