| DOI | Resolve DOI: https://doi.org/10.1088/0026-1394/57/1A/08014 |
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| Author | Search for: Josephs, R. D.; Search for: Li, M.; Search for: Daireaux, A.; Search for: Choteau, T.; Search for: Martos, G.; Search for: Westwood, S.; Search for: Wielgosz, R. I.; Search for: Li, H.; Search for: Wang, S.; Search for: Li, X.; Search for: Shi, N.; Search for: Wu, P.; Search for: Feng, L.; Search for: Huang, T.; Search for: Zhang, T.; Search for: Li, S.; Search for: Beltrão,, P. J.; Search for: Saraiva, A. Marcos; Search for: Garrido, B. C.; Search for: Scapin, S. M. Naressi; Search for: Wollinger, W.; Search for: Sade, Y. Bacila; Search for: Thibeault, M. -P.1; Search for: Stocks, B. B.1; Search for: Melanson, J. E.1; Search for: Kinumi, T.; Search for: Rezali, M. F. Bin; Search for: Öztug, M.; Search for: Akgöz, M.; Search for: Quaglia, M. |
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| Affiliation | - National Research Council of Canada. Metrology Research Centre
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| Format | Text, Article |
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| Physical description | 40 p. |
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| Abstract | Under the auspices of the Protein Analysis Working Group (PAWG) of the Comité Consultatif pour la Quantité de Matière (CCQM) a key comparison, CCQM-K115.b, was coordinated by the Bureau International des Poids et Mesures (BIPM) and the Chinese National Institute of Metrology (NIM). Seven Metrology Institutes or Designated Institutes and the BIPM participated. Participants were required to assign the mass fraction of oxytocin (OXT) present as the main component in the comparison sample for CCQM-K115.b. The comparison samples were prepared from synthetic OXT purchased from a commercial supplier and used as provided without further treatment or purification.
OXT was selected to be representative of the performance of a laboratory's measurement capability for the purity assignment of chemically synthesized peptides of known sequence, with one cross-link and up to 5 kDa. It was anticipated to provide an analytical measurement challenge representative for the value-assignment of compounds of broadly similar structural characteristics.
The majority of participants used amino acid analysis (PICAA) or quantitative nuclear magnetic resonance (PICqNMR) spectroscopy with a correction for structurally-related peptide impurities approach as the amount of material that has been provided to each participant (25 mg) is insufficient to perform a full mass balance based characterization of the material by a participating laboratory. The coordinators, both the BIPM and the NIM, were the laboratories to use the mass balance approach as they had more material available.
It was decided to propose KCRVs for both the OXT mass fraction and the mass fraction of the peptide related impurities as indispensable contributor regardless of the use of PICAA, PICqNMR or mass balance to determine the OXT purity. This allowed participants to demonstrate the efficacy of their implementation of the approaches used to determine the OXT mass fraction. In particular, it allows participants to demonstrate the efficacy of their implementation of peptide related impurity identification and quantification.
More detailed studies on the identification/quantification of peptide related impurities and the hydrolysis efficiency revealed that the integrity of the impurity profile of the related peptide impurities obtained by the participant is crucial for the impact on accuracy of the OXT mass fraction assignment. |
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| Publication date | 2020-01 |
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| Publisher | IOP |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 40272208-5f84-4635-aebf-5284b5f52c82 |
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| Record created | 2022-07-29 |
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| Record modified | 2022-07-29 |
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