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Methionine Alkylation as an Approach to Quantify Methionine Oxidation Using Mass Spectrometry.

Margaret Hoare1, Ruiyue Tan1, Kevin A Welle2

  • 1Department of Biology, University of Rochester, Rochester, New York 14627, United States.

Journal of the American Society for Mass Spectrometry
|February 7, 2024
PubMed
Summary

Quantifying methionine oxidation in proteins is difficult due to artifactual oxidation during analysis. A new mass spectrometry method, Methionine Oxidation by Blocking with Alkylation (MObBa), overcomes this by blocking unoxidized methionines.

Keywords:
mass spectrometry (MS)methionine alkylationmethionine oxidationproteomics

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Area of Science:

  • Biochemistry
  • Proteomics
  • Analytical Chemistry

Background:

  • Methionine oxidation is a post-translational modification affecting protein stability and function.
  • Accurate quantitation of methionine oxidation is challenging due to analytical artifacts.
  • Oxidation levels provide insights into protein structural integrity and regulation.

Purpose of the Study:

  • To develop a robust mass spectrometry-based method for quantifying methionine oxidation.
  • To overcome challenges associated with artifactual methionine oxidation during analysis.
  • To provide a reliable tool for assessing protein oxidation states.

Main Methods:

  • Developed Methionine Oxidation by Blocking with Alkylation (MObBa) method.
  • Utilized selective alkylation to block unoxidized methionine residues.
  • Employed mass spectrometry for quantitation of modified peptides.

Main Results:

  • MObBa successfully quantifies methionine oxidation by using alkylated methionines as stable proxies.
  • Demonstrated proof of concept in individual synthetic peptides.
  • Validated MObBa for proteome-wide scale methionine oxidation measurements.

Conclusions:

  • MObBa offers a straightforward experimental strategy for mass spectrometric quantitation of methionine oxidation.
  • This method enables accurate assessment of protein oxidation levels.
  • MObBa has potential applications in studying protein regulation and oxidative stress.