| Autor: |
García-Aranda MI; Instituto de Química Médica, CSIC, C/Juan de la Cierva 3, 28006 Madrid, Spain., González-López S, Santiveri CM, Gagey-Eilstein N, Reille-Seroussi M, Martín-Martínez M, Inguimbert N, Vidal M, García-López MT, Jiménez MA, González-Muñiz R, Pérez de Vega MJ |
| Jazyk: |
angličtina |
| Zdroj: |
Organic & biomolecular chemistry [Org Biomol Chem] 2013 Mar 21; Vol. 11 (11), pp. 1896-905. Date of Electronic Publication: 2013 Feb 04. |
| DOI: |
10.1039/c3ob27312a |
| Abstrakt: |
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: |
MEDLINE |
| Externí odkaz: |
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