Affinity adsorbent based on combinatorial phage display peptides that bind alpha-cobratoxin

J Chromatogr B Analyt Technol Biomed Life Sci. 2004 Jun 15;805(2):361-3. doi: 10.1016/j.jchromb.2004.03.019.

Abstract

Combinatorial phage display was used to discover peptides that selectively bind to the alpha-cobratoxin (neurotoxin) component of the multi-component venom of the Thai cobra, Naja kaouthia. Peptide sequences determined in this way were synthesized chemically and were covalently attached to agarose through the alpha-amino terminus. Such affinity chromatography supports selectively bound the alpha-cobratoxin component from crude venom, while passage of the crude venom over the support selectively depleted the venom of this component. The selective binding of alpha-cobratoxin to peptide-based solid-phase supports suggests that a limitless variety of peptides similarly obtained by combinatorial phage display can be used to craft specific analytical and preparative tools.

MeSH terms

  • Adsorption
  • Amino Acid Sequence
  • Bacteriophages / genetics*
  • Base Sequence
  • Chromatography, Affinity / instrumentation*
  • Cobra Neurotoxin Proteins / genetics
  • Cobra Neurotoxin Proteins / metabolism*
  • DNA Primers
  • Electrophoresis, Polyacrylamide Gel
  • Molecular Sequence Data
  • Peptides / chemistry
  • Peptides / metabolism*
  • Protein Binding

Substances

  • Cobra Neurotoxin Proteins
  • DNA Primers
  • Peptides
  • alpha-cobratoxin