1423138-52-6Relevant articles and documents
Helical peptides from VEGF and Vammin hotspots for modulating the VEGF-VEGFR interaction
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-Mu?iz, Rosario,De Vega, María Jesús Pérez
supporting information, p. 1896 - 1905 (2013/04/10)
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.
