Study summary · research use only
Investigating the detection of the novel doping‐relevant peptide kisspeptin‐10 in urine using liquid chromatography high‐resolution mass spectrometry
Plain-language summary
Paraphrased from the published abstract below — not a verdict on whether anything works.
This method-validation study developed a screening procedure and a confirmation procedure for detecting the peptide hormone kisspeptin-10 in human urine using liquid chromatography-mass spectrometry, for anti-doping purposes (kisspeptin-10 is on the 2024 World Anti-Doping Agency Prohibited List). Kisspeptin-10 was incubated in human serum to mimic metabolism, following prior research reporting a rapid elimination time of only 30 min after injection in rats. Four metabolites, corresponding to peptide fragments y9, y8, y7, and y5, were identified and added to the testing procedure. A degradation product was attributed to oxidation of a tryptophan residue into a kynurenine residue. Using the validated procedure, a black-market vial of kisspeptin-10 was analyzed and found to contain no unexpected impurities, though it showed more degradation than the purchased reference standard.
Abstract
Kisspeptin-10 is a peptide hormone capable of increasing circulating follicle-stimulating hormone, luteinizing hormone and testosterone levels in humans. Clinically, these effects suggest its use as a treatment for infertility. However, its testosterone-increasing effect indicates potential misuse in sports. As such, it is included in the 2024 World Anti-Doping Agency Prohibited List. This work describes the successful validation of an initial testing procedure (screening) and a confirmation procedure for kisspeptin-10 in urine using liquid chromatography-mass spectrometry. Additionally, kisspeptin-10 was incubated in human serum to mimic endogenous metabolism to improve method sensitivity, as previous research had demonstrated a rapid elimination time of only 30 min after injection (in rats). Four metabolites, corresponding to peptide fragments y9, y8, y7 and y5, were found and added to the ITP in full scan mode. A degradation product discovered during early experimentation was found to probably be caused by oxidation of the tryptophan residue into a kynurenine residue. Further research should elucidate the kinetic parameters of the reaction to improve product stability. Using the validated confirmation procedure, a black-market vial of kisspeptin-10 was analysed. The product contained no unexpected impurities, although it appeared to have undergone more degradation than the purchased reference standard.
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