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

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...

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Bibliographic Details
Published in:Analytical and bioanalytical chemistry 2022-09, Vol.414 (23), p.6761-6769
Main Authors: Reinders, Lars M. H., Klassen, Martin D., Teutenberg, Thorsten, Jaeger, Martin, Schmidt, Torsten C.
Format: Article
Language:English
Subjects:
Affinity
Affinity chromatography
Analytical Chemistry
Analytical methods
Biochemistry
Biological products
Characterization and Evaluation of Materials
Chemistry
Chemistry and Materials Science
Chromatography
Comparative analysis
Fc receptors
Food Science
Glycan
High performance liquid chromatography
High resolution
Laboratory Medicine
Liquid chromatography
Manufacturing industry
Mass spectrometry
Mass spectroscopy
Mathematical analysis
Monitoring/Environmental Analysis
Monoclonal antibodies
Orthogonality
Peptide mapping
Peptides
Research Paper
Rituximab
Scientific imaging
Spectroscopy
Structure-function relationships
Trastuzumab
Two dimensional analysis
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Summary: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. Graphical abstract
ISSN:1618-2642
1618-2650
DOI:10.1007/s00216-022-04236-8