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Related Experiment Videos

Mass tagging approach for mitochondrial thiol proteins.

Kevin Marley1, Duane T Mooney, Gretchen Clark-Scannell

  • 1Department of Chemistry, Oregon State University, Corvallis, OR 97331, USA.

Journal of Proteome Research
|August 9, 2005
PubMed
Summary

A novel mass tagging method uses stable isotope-coded reagents to label mitochondrial thiol proteins. This approach enables quantitative analysis and may help identify proteins susceptible to oxidative damage in redox proteomics.

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Area of Science:

  • Biochemistry
  • Proteomics
  • Analytical Chemistry

Background:

  • Mitochondrial thiol proteins play crucial roles in cellular respiration and are susceptible to oxidative modifications.
  • Accurate identification and quantification of these thiol proteins are essential for understanding mitochondrial function and disease.

Purpose of the Study:

  • To develop and validate a mass tagging approach for labeling mitochondrial thiol proteins under nondenaturing conditions.
  • To evaluate the utility of this approach for quantitative proteomics and identifying redox-sensitive thiols.

Main Methods:

  • Utilized stable isotope-coded, thiol-reactive (4-iodobutyl)triphenylphosphonium (IBTP) reagents (IBTP-d(0) and IBTP-d(15)).
  • Analyzed IBTP-labeled peptides using ESI-q-TOF and MALDI-TOF/TOF mass spectrometry.

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  • Applied the IBTP labeling strategy to cardiac mitochondrial protein extracts.

    • Main Results:

    • Low-energy CID in qTOF yielded suitable sequence tags for database searching.
    • High-energy CID in TOF/TOF caused fragmentation of the phosphonium moiety.
    • Demonstrated an average peptide quantitation variability of approximately 10% for d(0)/d(15)-tagged pairs.
    • Observed a potential bias of IBTP reagents towards surface-exposed protein thiols.

    Conclusions:

    • The IBTP mass tagging approach is effective for labeling and quantifying mitochondrial thiol proteins.
    • This method shows promise for redox proteomics, particularly for identifying thiols prone to oxidative modification.