Impurity determination for hepcidin by liquid chromatography-high resolution and ion mobility mass spectrometry for the value assignment of candidate primary calibrators

Anal Bioanal Chem. 2017 Apr;409(10):2559-2567. doi: 10.1007/s00216-017-0202-4. Epub 2017 Jan 30.

Abstract

In metrology institutes, the state-of-the-art for purity analysis of peptides/proteins mainly addresses short and unfolded peptides. Important developments are anticipated for the characterization of nonlinear peptides or proteins. Hepcidin 1-25 is an interesting model system because this small protein contains four disulfide bridges with a particular connectivity that is difficult to reproduce and could induce a bias in quantification. Hepcidin 1-25 is involved in iron-related disorders and anemia, in an inflammatory context, and its clinical relevance in neurodegenerative disorders is under investigation. It is also an emerging biomarker. Recent inter-laboratory studies showed a need for standardization of hepcidin assay and the need to produce certified reference materials. This paper discusses two hepcidin standards from different synthesis pathways that have been characterized by high-resolution mass spectrometry and ion mobility mass spectrometry.

Keywords: Disulfide bridges; Hepcidin; High-resolution mass spectrometry; Ion mobility, conformers; Purity assessment.

MeSH terms

  • Calibration
  • Chromatography, Liquid / methods*
  • Chromatography, Liquid / standards*
  • Drug Contamination / prevention & control*
  • Hepcidins / analysis*
  • Hepcidins / isolation & purification*
  • Humans
  • Mass Spectrometry / methods*
  • Mass Spectrometry / standards*
  • Reference Standards

Substances

  • Hepcidins