ArticlemAbs2016
Characterization of mAb dimers reveals predominant dimer forms common in therapeutic mAbs.
Article in mAbs, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Benchmarking Automated Mass Photometry against SEC-MALS and AUC for Quantifying Cross-Linked Monoclonal Antibody Aggregates.The AAPS journal · 2026Article
- Optical imaging and spectroscopic characterization of subvisible particles in protein therapeutics.Advanced drug delivery reviews · 2026Review
- Insights into the structural differences between homo- and heterodimers enriched from a cocktail of monoclonal antibodies against SARS-CoV-2.Scientific reports · 2026Article
- Optimization of Radiolabeling of a [Cancers · 2023Article
- Article
- Development and Biophysical Characterization of a Humanized FSH-Blocking Monoclonal Antibody Therapeutic Formulated at an Ultra-High Concentration.bioRxiv : the preprint server for biology · 2023Article
- The Relationship between Protein-Protein Interactions and Liquid-Liquid Phase Separation for Monoclonal Antibodies.Molecular pharmaceutics · 2023Article
- Antibody Conjugates Bispecific for Pollen Allergens and ICAM-1 with Potential to Prevent Epithelial Allergen Transmigration and Rhinovirus Infection.International journal of molecular sciences · 2023Article
- Identification of Hetero-aggregates in Antibody Co-formulations by Multi-dimensional Liquid Chromatography Coupled to Mass Spectrometry.Analytical chemistry · 2023Article
- Development of a scalable single process for producing SARS-CoV-2 RBD monomer and dimer vaccine antigens.Frontiers in bioengineering and biotechnology · 2023Article
- Effects of Monovalent Salt on Protein-Protein Interactions of Dilute and Concentrated Monoclonal Antibody Formulations.Antibodies (Basel, Switzerland) · 2022Article
- Detection of Isopeptide Bonds in Monoclonal Antibody Aggregates.Pharmaceutical research · 2021Article
- Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies.Cell · 2021Article
- Sedimentation Velocity Analytical Ultracentrifugation Analysis of Marketed Rituximab Drug Product Size Distribution.Pharmaceutical research · 2020Article
- Structural basis of polyethylene glycol recognition by antibody.Journal of biomedical science · 2020Article
- Light-induced complex formation of bacteriophytochrome RpBphP1 and gene repressor RpPpsR2 probed by SAXS.The FEBS journal · 2019Article
- Article
- Rapid screening of IgG quality attributes - effects on Fc receptor binding.FEBS open bio · 2017Article
- Article
- Article
Corrections and comments
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Authors and funding
13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formation of undesired high molecular weight species such as dimers is an important quality attribute for therapeutic monoclonal antibody formulations. Therefore, the thorough understanding of mAb dimerization and the detailed characterization mAb dimers is of great interest for future pharmaceutical development of therapeutic antibodies. In this work, we focused on the analyses of different mAb dimers regarding size, surface properties, chemical identity, overall structure and localization of possible dimerization sites. Dimer fractions of different mAbs were isolated to a satisfactory purity from bulk material and revealed 2 predominant overall structures, namely elongated and compact dimer forms. The elongated dimers displayed one dimerization site involving the tip of the Fab domain. Depending on the stress applied, these elongated dimers are connected either covalently or non-covalently. In contrast, the compact dimers exhibited non-covalent association. Several interaction points were detected for the compact dimers involving the hinge region or the base of the Fab domain. These results indicate that mAb dimer fractions are rather complex and may contain more than one kind of dimer. Nevertheless, the overall appearance of mAb dimers suggests the existence of 2 predominant dimeric structures, elongated and compact, which are commonly present in preparations of therapeutic mAbs.
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