Total chemical synthesis of the D2 domain of human VEGF receptor 1
2009
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.
Keywords:
- Correction
- Source
- Cite
- Save
- Machine Reading By IdeaReader
18
References
8
Citations
NaN
KQI