Physicochemical characterization of Remsima®
| Autor: | Soon Kwan Jung, Joon Won Lee, Jae Won Jeon, Kyoung Hoon Lee, Dong-Il Kim, Shin Jae Chang, Jin Soo Bae, Soo Young Lee, Yeon Jung Kim, Byoung Oh Kwon |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular Glycan Glycosylation Chemical Phenomena medicine.drug_class Protein Conformation Immunology Apoptosis Pharmacology Monoclonal antibody Crystallography X-Ray Peptide Mapping Mass Spectrometry Jurkat Cells Biosimilar Pharmaceuticals In vivo Spectroscopy Fourier Transform Infrared medicine Immunology and Allergy Potency media_common.cataloged_instance Humans characterization comparability European union Drug Approval Chromatography High Pressure Liquid media_common biology Calorimetry Differential Scanning Chemistry Circular Dichroism reference medicinal product (RMP) Antibodies Monoclonal Biosimilar In vitro Infliximab biology.protein biosimilar Remicade® CT-P13 Remsima® Reports |
| Zdroj: | mAbs |
| ISSN: | 1942-0870 1942-0862 |
| Popis: | Remsima® (infliximab) was recently approved as the world's first biosimilar monoclonal antibody (mAb) in both the European Union and Korea. To achieve this, extensive physicochemical characterization of Remsima® in relation to Remicade® was conducted in order to demonstrate the highly similar properties between the two molecules. A multitude of state-of-the-art analyses revealed that Remsima® has identical primary as well as indistinguishable higher order structures compared with the original product. Monomer and aggregate contents of Remsima® were also found to be comparable with those of Remicade®. In terms of charge isoforms, although Remsima® was observed to contain slightly less basic variants than the original antibody, the difference was shown to be largely due to the presence of C-terminal lysine. On the other hand, this lysine was found to be rapidly clipped inside serum in vitro and in vivo, suggesting it has no effect on the biological potency or safety of the drug. Analysis of the glycan contents of the antibodies showed comparable glycan types and distributions. Recent results of clinical studies have further confirmed that the two antibody products are highly similar to each other. Based on this research as well as previous clinical and non-clinical comparability studies, Remsima® can be considered as a highly similar molecule to Remicade® in terms of physicochemical properties, efficacy, and safety for its final approval as a biosimilar product to Remicade®. |
| Databáze: | OpenAIRE |
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