Functional binding surface of a β-hairpin VEGF receptor targeting peptide determined by NMR spectroscopy in living cells

Chemistry. 2015 Jan 2;21(1):91-5. doi: 10.1002/chem.201403335. Epub 2014 Nov 6.

Abstract

In this study, the functional interaction of HPLW peptide with VEGFR2 (Vascular Endothelial Growth Factor Receptor 2) was determined by using fast (15)N-edited NMR spectroscopic experiments. To this aim, (15)N uniformly labelled HPLW has been added to Porcine Aortic Endothelial Cells. The acquisition of isotope-edited NMR spectroscopic experiments, including (15)N relaxation measurements, allowed a precise characterization of the in-cell HPLW epitope recognized by VEGFR2.

Keywords: 15N labelled peptides; NMR spectroscopy; VEGF receptors; living cells; peptide-protein interaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Nitrogen Isotopes / chemistry
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptides / chemistry*
  • Peptides / metabolism
  • Protein Interaction Domains and Motifs
  • Protein Structure, Secondary
  • Swine
  • Vascular Endothelial Growth Factor Receptor-2 / agonists*
  • Vascular Endothelial Growth Factor Receptor-2 / genetics
  • Vascular Endothelial Growth Factor Receptor-2 / metabolism

Substances

  • Nitrogen Isotopes
  • Peptides
  • Vascular Endothelial Growth Factor Receptor-2