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Element-coded affinity tags for peptides and proteins.

Paul A Whetstone1, Nathaniel G Butlin, Todd M Corneillie

  • 1Department of Chemistry, University of California, One Shields Avenue, Davis, California 95616, USA.

Bioconjugate Chemistry
|January 22, 2004
PubMed
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Researchers developed a novel element-coded metal chelate labeling technique for protein analysis. This method enables affinity purification, quantification, and identification of tagged peptides in complex biological mixtures.

Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Biochemistry

Background:

  • Isotope-coded affinity tags (ICAT) are established tools for protein mixture analysis.
  • Existing methods face challenges in purification, quantification, and identification within complex biological systems.

Purpose of the Study:

  • To develop an alternative protein-labeling technique using element-coded metal chelates.
  • To demonstrate affinity chromatography, quantification, and identification of tagged peptides.

Main Methods:

  • Synthetic peptides were modified with carboxymethyl or element-coded metal chelates (terbium, yttrium).
  • A mixture of modified peptides underwent trypsinization and purification using a novel affinity column for rare-earth DOTA chelates.
  • Analysis was performed using Liquid Chromatography-Mass Spectrometry/Mass Spectrometry (LC-MS/MS).

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Main Results:

  • Chelate-tagged tryptic peptides were successfully purified and eluted from the affinity column.
  • Tagged peptides coeluted chromatographically and were present in the expected ratios via MS ion intensity.
  • Peptide sequences were confirmed using tandem mass spectrometry.

Conclusions:

  • DOTA-rare earth chelates exhibit excellent properties for affinity tagging, including high polarity and water solubility.
  • Monoisotopic rare earth elements offer diverse options for creating mass tags.
  • The mass defects of heavy rare earth elements provide precise mass values for tagged peptides, aiding identification.