Comparison of originator and biosimilar monoclonal antibodies using HRMS, Fc affinity chromatography, and 2D-HPLC.

Autor: Reinders LMH; Institut Für Energie- und Umwelttechnik e. V. (IUTA, Institute of Energy and Environmental Technology), Bliersheimer Str. 58-60, 47229, Duisburg, Germany.; Hochschule Niederrhein (University of Applied Science), Reinarzstr. 49, 47805, Krefeld, Germany.; Instrumental Analytical Chemistry, Faculty of Chemistry, University Duisburg-Essen, Universitätsstr. 5, 45141, Essen, Germany., Klassen MD; Institut Für Energie- und Umwelttechnik e. V. (IUTA, Institute of Energy and Environmental Technology), Bliersheimer Str. 58-60, 47229, Duisburg, Germany., Teutenberg T; Institut Für Energie- und Umwelttechnik e. V. (IUTA, Institute of Energy and Environmental Technology), Bliersheimer Str. 58-60, 47229, Duisburg, Germany. teutenberg@iuta.de., Jaeger M; Hochschule Niederrhein (University of Applied Science), Reinarzstr. 49, 47805, Krefeld, Germany., Schmidt TC; Instrumental Analytical Chemistry, Faculty of Chemistry, University Duisburg-Essen, Universitätsstr. 5, 45141, Essen, Germany.
Jazyk: angličtina
Zdroj: Analytical and bioanalytical chemistry [Anal Bioanal Chem] 2022 Sep; Vol. 414 (23), pp. 6761-6769. Date of Electronic Publication: 2022 Jul 27.
DOI: 10.1007/s00216-022-04236-8
Abstrakt: Due to the complex manufacturing process of therapeutic monoclonal antibodies, it is hardly possible to produce an identical copy of the original product (originator). Consequently, follow-on products (biosimilars) must demonstrate their efficacy being similar to the originator in terms of structure and function. During this process, a variety of analytical methods are required for this purpose. This study focuses on three particularly relevant analytical techniques: high-resolution mass spectrometry, fragment crystallisable (Fc) affinity chromatography, and two-dimensional peptide mapping. Each analytical method proved able to identify specific differences between originator and biosimilar. High-resolution mass spectrometry was used to characterize the glycan pattern. It was shown that a trastuzumab biosimilar did not have the G0:G0F sugar modification identified in the originator. The application of affinity chromatography to rituximab showed that originator and biosimilar interacted differently with the immobilized Fc receptor. Furthermore, 2D-HPLC peptide mapping demonstrated the influence of orthogonality of separation dimensions, leading to differentiation of a rituximab originator and biosimilar.
(© 2022. Springer-Verlag GmbH Germany, part of Springer Nature.)
Databáze: MEDLINE
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