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A peptoid "antibody surrogate" that antagonizes VEGF receptor 2 activity

Academic Article
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Overview

authors

  • Udugamasooriya, D. G.
  • Dineen, S. P.
  • Brekken, R. A.
  • Kodadek, Thomas

publication date

  • April 2008

journal

  • Journal of the American Chemical Society  Journal

abstract

  • We report a two-color, cell-based screen to identify specific receptor-binding compounds in a combinatorial library of peptoids displayed on beads. We apply this strategy to the isolation of vascular endothelial growth factor receptor 2 (VEGFR2)-binding peptoids. A dimeric derivative of one of these lead compounds is shown to be an antagonist of VEGFR2 activity both in vitro and in vivo. This methodology provides a potentially general route to synthetic molecules that bind integral membrane receptors with affinities and specificities similar to those of antibodies, but which are far smaller and easier to make and manipulate.

subject areas

  • Animals
  • Antibodies, Monoclonal
  • Binding Sites
  • Cell Membrane
  • Cells, Cultured
  • Chromatography, High Pressure Liquid
  • Dimerization
  • Humans
  • Immunohistochemistry
  • Ligands
  • Peptoids
  • Vascular Endothelial Growth Factor Receptor-2
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Identity

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja711193x

PubMed ID

  • 18386897
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Additional Document Info

start page

  • 5744

end page

  • 5752

volume

  • 130

issue

  • 17

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