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Repurposing the Pummerer Rearrangement: Determination of Methionine Sulfoxides in Peptides

  1. Author:
    Woodroofe, Carolyn C.
    Ivanic,Joseph
    Monti, Sarah
    Levine, Rodney L.
    Swenson, Rolf E.

  2. Author Address

    NHLBI, Imaging Probe Dev Ctr, NIH, 9800 Med Ctr Dr, Rockville, MD 20850 USA.Leidos Biomed Res Inc, Frederick Natl Lab Canc Res, Adv Biomed Computat Sci Grp, 1011 Beasley Dr, Frederick, MD 21701 USA.NHLBI, Lab Biochem, NIH, 50 South Dr, Bethesda, MD 20892 USA.
    1. Year: 2019
    2. Date: OCT 25
  2. Journal: CHEMBIOCHEM
  3. WILEY-V C H VERLAG GMBH,
  5. Type of Article: Article
  6. ISSN: 1439-4227
  1. Abstract:

    The reversible oxidation of methionine residues in proteins has emerged as a biologically important post-translational modification. However, detection and quantitation of methionine sulfoxide in proteins is difficult. Our aim is to develop a method for specifically derivatizing methionine sulfoxide residues. We report a Pummerer rearrangement of methionine sulfoxide treated sequentially with trimethylsilyl chloride and then 2-mercaptoimidazole or pyridine-2-thiol to produce a dithioacetal product. This derivative is stable to standard mass spectrometry conditions, and its formation identified oxidized methionine residues. The scope and requirements of dithioacetal formation are reported for methionine sulfoxide and model substrates. The reaction intermediates have been investigated by computational techniques and by C-13 NMR spectroscopy. These provide evidence for an alpha-chlorinated intermediate. The derivatization allows for detection and quantitation of methionine sulfoxide in proteins by mass spectrometry and potentially by immunochemical methods.

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External Sources

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  2. DOI: 10.1002/cbic.201900463
  3. View record in Web of Science®
  4. WOS: 000492389400001

Library Notes

  1. Fiscal Year: FY2019-2020
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