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Total chemical synthesis of the D2 domain of human VEGF receptor 1
Author(s) -
Goncalves Victor,
Gautier Benoit,
Huguenot Florent,
Leproux Pascale,
Garbay Christiane,
Vidal Michel,
Inguimbert Nicolas
Publication year - 2009
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1133
Subject(s) - angiogenesis , receptor , vegf receptors , vascular endothelial growth factor , chemistry , peptide , kinase insert domain receptor , microbiology and biotechnology , folding (dsp implementation) , cancer research , biochemistry , pharmacology , vascular endothelial growth factor a , biology , electrical engineering , engineering
Abstract The interaction of the vascular endothelial growth factor (VEGF) with its cellular receptors exerts a central role in the regulation of angiogenesis. Among these receptors, the VEGF receptor 1 may be implicated in pathological angiogenesis. Here, we report the first total chemical synthesis of the VEGF‐binding domain of the VEGF receptor 1. Aggregation issues were overcome by the use of a low‐substituted resin and the stepwise introduction of pseudoproline dipeptides and Dmb‐glycines. The folding of the protein was achieved by air oxidation and its biological activity was verified on ELISA‐based assays. Copyright © 2009 European Peptide Society and John Wiley & Sons, Ltd.