Alternative LC/ESI-MS/MS approach to screen hemoglobin N-terminal modifications

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Abstract

Proteins are continuously exposed to reactive chemical species owing to physiological and chemical stresses, resulting in various chemical modifications such as oxidation, nitration, glycation/glycoxidation, lipidation/lipoxidation, and adduct formation with drugs/chemicals. Hemoglobin (Hb) is the most abundant protein in blood (∼150 mg/mL) with a long half-life (turnover: 126 days). Hb is thus believed to be a major target of reactive chemical species and those modifications reflect biological events. Chemical modifications on Hb have been analyzed as N-terminal valine (Val) adducts by the Edman degradation reaction because Val is the N-terminal amino acid in both the α- and β-subunits of Hb and is exposed on the surface of the protein. However, this strategy is limited to N-terminal alkylated Val and overlooks N-terminal acylated and deaminated Val. Here, we describe a proof-of-concept study to develop an alternative screening approach based on liquid chromatography-tandem mass spectrometry with peptide-specific constant neutral loss/precursor ion scanning to include all types of N-terminal modifications on Hb.

Original languageEnglish
Article number116651
JournalInternational Journal of Mass Spectrometry
Volume468
DOIs
Publication statusPublished - 2021 Oct

Keywords

  • Chemical modifications
  • Hemoglobin
  • Mass spectrometry
  • N-Terminal modifications

ASJC Scopus subject areas

  • Instrumentation
  • Condensed Matter Physics
  • Spectroscopy
  • Physical and Theoretical Chemistry

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