VEGFR Recognition Interface of a Proangiogenic VEGF-Mimetic Peptide Determined In Vitro and in the Presence of Endothelial Cells by NMR Spectroscopy

Chemistry. 2018 Aug 6;24(44):11461-11466. doi: 10.1002/chem.201802117. Epub 2018 Jul 9.

Abstract

QK peptide is a vascular endothelial growth factor (VEGF)-mimetic molecule with significant proangiogenic activity. In particular, QK is able to bind and activate VEGF receptors (VEGFRs) to stimulate a functional response in endothelial cells. To characterize the peptide bioactivity and its molecular recognition properties, a detailed picture of the interaction between peptide QK and VEGF receptors is reported. By combining NMR spectroscopy studies in solution on the purified receptor and in the presence of intact endothelial cells, a molecular description of the binding interaction between peptide QK and VEGFR2 in the cellular context is obtained. These results reveal useful insights into the peptide biological mechanism, which opens the way to further optimization of this class of VEGF-mimicking peptides.

Keywords: NMR spectroscopy; angiogenesis; noncovalent interactions; peptides; receptors.

MeSH terms

  • Biomimetic Materials / chemistry*
  • Endothelial Cells
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Peptides / chemistry*
  • Protein Binding
  • Protein Conformation
  • Receptors, Vascular Endothelial Growth Factor / chemistry*
  • Vascular Endothelial Growth Factor A / chemistry*

Substances

  • Peptides
  • QK VEGF mimetic peptide
  • Vascular Endothelial Growth Factor A
  • Receptors, Vascular Endothelial Growth Factor