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

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.
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https://hal.umontpellier.fr/hal-01785651
Contributeur : Mélanie Karli <>
Soumis le : vendredi 4 mai 2018 - 14:47:37
Dernière modification le : mardi 28 mai 2019 - 17:04:08

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Pauline Bros, Ralf Josephs, Norbert Stoppacher, Guillaume Cazals, Sylvain Lehmann, et al.. Impurity determination for hepcidin by liquid chromatography-high resolution and ion mobility mass spectrometry for the value assignment of candidate primary calibrators. Analytical and Bioanalytical Chemistry, Springer Verlag, 2017, 409 (10), pp.2559 - 2567. ⟨10.1007/s00216-017-0202-4⟩. ⟨hal-01785651⟩

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