Comparing the original and biosimilar biotherapeutics of the monoclonal antibody eculizumab by intact mass measurement and middle-up mass spectrometry analysis
Objectives. In this biosimilar research, we compare the monoclonal antibody eculizumab obtained from different drugs [original Soliris® (Alexion Pharmaceuticals) and candidate Elizaria® (Generium)] by intact mass measurement and middle-up mass spectrometry analysis to enhance the role of mass spectr...
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| Format: | Article |
| Language: | Russian |
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MIREA - Russian Technological University
2021-03-01
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| Series: | Тонкие химические технологии |
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| Online Access: | https://www.finechem-mirea.ru/jour/article/view/1688 |
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| author | M. B. Degterev R. R. Shukurov |
| author_facet | M. B. Degterev R. R. Shukurov |
| author_sort | M. B. Degterev |
| collection | DOAJ |
| description | Objectives. In this biosimilar research, we compare the monoclonal antibody eculizumab obtained from different drugs [original Soliris® (Alexion Pharmaceuticals) and candidate Elizaria® (Generium)] by intact mass measurement and middle-up mass spectrometry analysis to enhance the role of mass spectrometry methods in biopharmaceutical development processes.Methods. The intact mass measurement is performed using a high-resolution ESI-MS. The middle-up analysis is performed by reversed-phase high-performance liquid chromatography with ESI-MS detection, subsequent IdeS treatment of antibodies, and disulfide bond reduction.Results. We have shown some small differences between the original and candidate drugs in the minor glycans level. Man5 glycan is only found in the original Soliris, and G0 is only found in the Elizaria. Glycation sites are also found in the light chain and Fd subunits of the original Soliris. The glycation level does not exceed 4.4%. The non-clipped C-end lysine level and G0F glycan levels are slightly lower in the original Soliris. All registered differences are not crucial for eculizumab’s quality and do not affect its effectiveness and preclinical safety. Generally, the results show a high level of similarity between the original and candidate drugs.Conclusions. The comparative mass spectrometry analysis of eculizumab in the original Soliris and Elizaria allows us to estimate their high degree of similarity by molecular masses and major modification profiles. |
| format | Article |
| id | doaj-art-22bab6db8fc24fed806631dff24d4c1b |
| institution | DOAJ |
| issn | 2410-6593 2686-7575 |
| language | Russian |
| publishDate | 2021-03-01 |
| publisher | MIREA - Russian Technological University |
| record_format | Article |
| series | Тонкие химические технологии |
| spelling | doaj-art-22bab6db8fc24fed806631dff24d4c1b2025-08-20T02:59:45ZrusMIREA - Russian Technological UniversityТонкие химические технологии2410-65932686-75752021-03-01161768710.32362/2410-6593-2021-16-1-76-871626Comparing the original and biosimilar biotherapeutics of the monoclonal antibody eculizumab by intact mass measurement and middle-up mass spectrometry analysisM. B. Degterev0R. R. Shukurov1International Biotechnology Center GeneriumInternational Biotechnology Center GeneriumObjectives. In this biosimilar research, we compare the monoclonal antibody eculizumab obtained from different drugs [original Soliris® (Alexion Pharmaceuticals) and candidate Elizaria® (Generium)] by intact mass measurement and middle-up mass spectrometry analysis to enhance the role of mass spectrometry methods in biopharmaceutical development processes.Methods. The intact mass measurement is performed using a high-resolution ESI-MS. The middle-up analysis is performed by reversed-phase high-performance liquid chromatography with ESI-MS detection, subsequent IdeS treatment of antibodies, and disulfide bond reduction.Results. We have shown some small differences between the original and candidate drugs in the minor glycans level. Man5 glycan is only found in the original Soliris, and G0 is only found in the Elizaria. Glycation sites are also found in the light chain and Fd subunits of the original Soliris. The glycation level does not exceed 4.4%. The non-clipped C-end lysine level and G0F glycan levels are slightly lower in the original Soliris. All registered differences are not crucial for eculizumab’s quality and do not affect its effectiveness and preclinical safety. Generally, the results show a high level of similarity between the original and candidate drugs.Conclusions. The comparative mass spectrometry analysis of eculizumab in the original Soliris and Elizaria allows us to estimate their high degree of similarity by molecular masses and major modification profiles.https://www.finechem-mirea.ru/jour/article/view/1688eculizumabmass spectrometryposttranslational modificationsbiosimilar drugsglycosylationhigh-performance liquid chromatography-mass spectrometryintact mass measurementmiddle-up analysismonoclonal antibody |
| spellingShingle | M. B. Degterev R. R. Shukurov Comparing the original and biosimilar biotherapeutics of the monoclonal antibody eculizumab by intact mass measurement and middle-up mass spectrometry analysis Тонкие химические технологии eculizumab mass spectrometry posttranslational modifications biosimilar drugs glycosylation high-performance liquid chromatography-mass spectrometry intact mass measurement middle-up analysis monoclonal antibody |
| title | Comparing the original and biosimilar biotherapeutics of the monoclonal antibody eculizumab by intact mass measurement and middle-up mass spectrometry analysis |
| title_full | Comparing the original and biosimilar biotherapeutics of the monoclonal antibody eculizumab by intact mass measurement and middle-up mass spectrometry analysis |
| title_fullStr | Comparing the original and biosimilar biotherapeutics of the monoclonal antibody eculizumab by intact mass measurement and middle-up mass spectrometry analysis |
| title_full_unstemmed | Comparing the original and biosimilar biotherapeutics of the monoclonal antibody eculizumab by intact mass measurement and middle-up mass spectrometry analysis |
| title_short | Comparing the original and biosimilar biotherapeutics of the monoclonal antibody eculizumab by intact mass measurement and middle-up mass spectrometry analysis |
| title_sort | comparing the original and biosimilar biotherapeutics of the monoclonal antibody eculizumab by intact mass measurement and middle up mass spectrometry analysis |
| topic | eculizumab mass spectrometry posttranslational modifications biosimilar drugs glycosylation high-performance liquid chromatography-mass spectrometry intact mass measurement middle-up analysis monoclonal antibody |
| url | https://www.finechem-mirea.ru/jour/article/view/1688 |
| work_keys_str_mv | AT mbdegterev comparingtheoriginalandbiosimilarbiotherapeuticsofthemonoclonalantibodyeculizumabbyintactmassmeasurementandmiddleupmassspectrometryanalysis AT rrshukurov comparingtheoriginalandbiosimilarbiotherapeuticsofthemonoclonalantibodyeculizumabbyintactmassmeasurementandmiddleupmassspectrometryanalysis |