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

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 prot...

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Veröffentlicht in:Analytical and bioanalytical chemistry 2017-04, Vol.409 (10), p.2559-2567
Hauptverfasser: Bros, Pauline, Josephs, Ralf D., Stoppacher, Norbert, Cazals, Guillaume, Lehmann, Sylvain, Hirtz, Christophe, Wielgosz, Robert I., Delatour, Vincent
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Sprache:eng
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Zusammenfassung: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.
ISSN:1618-2642
1618-2650
DOI:10.1007/s00216-017-0202-4