Journal
DRUG TESTING AND ANALYSIS
Volume 9, Issue 11-12, Pages 1799-1803Publisher
WILEY
DOI: 10.1002/dta.2306
Keywords
doping; high resolution mass spectrometry; peptide hormones; degradation products
Funding
- Manfred Donike Institute for Doping Analysis (Cologne, Germany)
- World Anti-Doping Agency (WADA) [15A22MT]
- Federal Ministry of the Interior of the Federal Republic of Germany (Bonn, Germany)
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With an increasing number of prohibited substances in doping controls, knowledge about their metabolism is crucial for efficient analysis. While for lowmolecularmassmolecules, standard protocols for in vitrometabolismexperiments are well established, the situation with peptidic drugs has been shown to be substantially more heterogeneous and complex. Two principle strategies aiming at simulating the metabolism of lower molecular mass peptides in vitro are presented within this study. The prohibited peptides ARA-290, GHRP-3, and Peforelin, with a to-date unknown metabolism, were chosen as model compounds for these experiments and metabolism after incubation with different blood specimens (DTA-, heparin-, citrate-plasma, and serum) and exposure to recombinant amidase were investigated. The characterization of in vitro generated drug-derived peptidic analytes was accomplished by means of liquid chromatography coupled to high resolutionmass spectrometry. Identification of the generated metabolites was ensured by dedicated high resolution product ion experiments after liquid chromatographic separation. While extensive exopeptidase-driven metabolism was observed for ARA-290 (with one main metabolite PyrEQLERALN), GHRP-3 and Peforelin were found to exhibit a considerable metabolic stability with a low tendency for deamidation only. Copyright (c) 2017 John Wiley & Sons, Ltd.
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