State-of-the-art and trends for the SI traceable value assignment of the purity of peptides using the model compound angiotensin I

Josephs, R D; Stoppacher, Norbert; Daireaux, Adeline; Choteau, Tiphaine; Lippa, Katrice A.; Phinney, Karen W.; Westwood, Steven; Wielgosz, Robert

doi:10.1016/j.trac.2017.09.026

Cited by 25 publications

(26 citation statements)

References 22 publications

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“…Peptides are widely applied in several fields of biological, biochemical, biomedical, and physiological research, for example, in the study and modeling of variable biomolecular interactions, such as hormone-receptor, drug-receptor, enzymesubstrate, enzyme-inhibitor, ion-ionophore, and antigenantibody, and in the identification of antigenic determinants (epitopes) of proteins. In addition, peptide and peptidomimetic drugs, and food and feed additives belong to the relevant compounds also in biotechnology, pharmaceutical, food and feed industry [196][197][198]. Consequently, there is a high need for qualitative and quantitative analysis of peptides by CE and other analytical methods.…”

Section: Quality Control and Determination Of Puritymentioning

confidence: 99%

Recent developments in capillary and microchip electroseparations of peptides (2019–mid 2021)

Kašička

2021

Electrophoresis

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The review provides a comprehensive overview of developments and applications of high performance capillary and microchip electroseparation methods (zone electrophoresis, isotachophoresis, isoelectric focusing, affinity electrophoresis, electrokinetic chromatography, and electrochromatography) for analysis, microscale isolation, and physicochemical characterization of peptides from 2019 up to approximately the middle of 2021. Advances in the investigation of electromigration properties of peptides and in the methodology of their analysis, such as sample preparation, sorption suppression, EOF control, and detection, are presented. New developments in the individual CE and CEC methods are demonstrated and several types of their applications are shown. They include qualitative and quantitative analysis, determination in complex biomatrices, monitoring of chemical and enzymatic reactions and physicochemical changes, amino acid, sequence, and chiral analyses, and peptide mapping of proteins. In addition, micropreparative separations and determination of significant physicochemical parameters of peptides by CE and CEC methods are described.

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Section: Quality Control and Determination Of Puritymentioning

confidence: 99%

Recent developments in capillary and microchip electroseparations of peptides (2019–mid 2021)

Kašička

2021

Electrophoresis

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“…However, a full mass balance approach could require unviably large quantities of peptide material. A simpler alternative to the full mass balance approach is a peptide impurity corrected amino acid (PICAA) analysis, requiring quantification of constituent amino acids following hydrolysis of the material and correction for amino acids originating from impurities [17][18]. It requires identification and quantification of peptide impurities for the most accurate results.…”

Section: Rationale/purposementioning

confidence: 99%

Pilot study on peptide purity—synthetic human C-peptide

Josephs

Song

et al. 2017

Metrologia

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Under the auspices of the Protein Analysis Working Group (PAWG) of the Comité Consultatif pour la Quantité de Matière (CCQM) a pilot study, CCQM-P55.2, was coordinated by the Bureau International des Poids et Mesures (BIPM) and the Chinese National Institute of Metrology (NIM). Four Metrology Institutes or Designated Institutes and the BIPM participated. Participants were required to assign the mass fraction of human C-peptide (hCP) present as the main component in the comparison sample for CCQM-P55.2. The comparison samples were prepared from synthetic human hCP purchased from a commercial supplier and used as provided without further treatment or purification. hCP was selected to be representative of the performance of a laboratory's measurement capability for the purity assignment of short (up to 5 kDa), non-cross-linked synthetic peptides/proteins. 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 a quantitative nuclear magnetic resonance spectroscopy (qNMR) corrected for peptide impurities. Other participants provided results obtained by peptide impurity corrected amino acid analysis (PICAA) or elemental analysis (PICCHN). It was decided to assign reference values based on the KCRVs of CCQM-K115 for both the hCP mass fraction and the mass fraction of the peptide related impurities as indispensable contributor regardless of the use of PICAA, mass balance or any other approach to determine the hCP purity. This allowed participants to demonstrate the efficacy of their implementation of the approaches used to determine the hCP mass fraction. In particular it allows participants to demonstrate the efficacy of their implementation of peptide related impurity identification and quantification. The assessment of the mass fraction of peptide impurities is based on the assumption that only the most exhaustive and elaborate set of results is taken for the calculation of the reference value. The reference value for the peptide related impurity mass fractions of the material was 83.3 mg/g with a combined standard uncertainty of 1.5 mg/g. Inspection of the degree of equivalence plots for the mass fraction of peptide impurities and additional information obtained from the peptide related impurity profile indicates that in many cases only a very small number of impurities have been identified and quantified resulting in an underestimation of the peptide related impurity mass fractions. The reference value for the mass fraction of hCP for CCQM-KP55.2 is 801.8 mg/g with a corresponding combined standard uncertainty of 3.1 mg/g. Inspection of the degree of equivalence plots for CCQM-P55.2 for the mass fraction of hCP shows that three results agree with the reference value. Main text To reach the main text of this paper, click on Final Report. The final report has been peer-reviewed and approved for publication by the CCQM.

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“…fraction, the measured isotope amount ratio, and the mass of solution, respectively. Validation of this technique has been demonstrated in inter-laboratory comparisons [22,23], and has facilitated purity assessment of multiple peptide RMs [24][25][26].…”

Section: Amino Acid Analysis By Lc-id-ms/msmentioning

confidence: 99%

Characterization of a SARS-CoV-2 spike protein reference material

2022

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Development of diagnostic testing capability has advanced with unprecedented pace in response to the COVID-19 pandemic. An undesirable effect of such speed is a lack of standardization, often leading to unreliable test results. To assist the research community surmount this challenge, the National Research Council Canada has prepared a SARS-CoV-2 spike protein reference material, SMT1-1, as a buffered solution. Value assignment was achieved by amino acid analysis (AAA) by double isotope dilution liquid chromatography–tandem mass spectrometry (LC-ID-MS/MS) following acid hydrolysis of the protein, in combination with ultraviolet–visible spectrophotometry (UV–Vis) based on tryptophan and tyrosine absorbance at 280 nm. Homogeneity of the material was established through spectrophotometric absorbance readings at 280 nm. Transportation and long-term storage stabilities were assessed by monitoring relative changes in oligomeric state by size-exclusion liquid chromatography (LC-SEC) with UV detection. The molar concentration of the spike protein in SMT1-1 was 5.68 ± 0.22 µmol L−1 (k = 2, 95% CI), with the native trimeric form accounting for ~ 94% of the relative abundance. Reference mass concentration and mass fraction values were calculated using the protein molecular weight and density of the SMT1-1 solution. The spike protein is highly glycosylated which leads to analyte ambiguity when reporting the more commonly used mass concentration. After glycoprotein molar mass determination by LC-SEC with multi-angle light scattering detection, we thus reported mass concentration values for both the protein-only portion and intact glycoprotein as 0.813 ± 0.030 and 1.050 ± 0.068 mg mL−1 (k = 2), respectively.

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State-of-the-art and trends for the SI traceable value assignment of the purity of peptides using the model compound angiotensin I

Cited by 25 publications

References 22 publications

Recent developments in capillary and microchip electroseparations of peptides (2019–mid 2021)

Recent developments in capillary and microchip electroseparations of peptides (2019–mid 2021)

Pilot study on peptide purity—synthetic human C-peptide

Characterization of a SARS-CoV-2 spike protein reference material

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