ArticlePharmaceutical research2012
Structure and function of purified monoclonal antibody dimers induced by different stress conditions.
Article in Pharmaceutical research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 80 citations in OpenAlex.
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- Modeling the behavior of monoclonal antibodies on hydrophobic interaction chromatography resins.Bioresources and bioprocessing · 2024Article
- Getting Smaller by Denaturation: Acid-Induced Compaction of Antibodies.The journal of physical chemistry letters · 2023Article
- Identification of Hetero-aggregates in Antibody Co-formulations by Multi-dimensional Liquid Chromatography Coupled to Mass Spectrometry.Analytical chemistry · 2023Article
- Analytical and Functional Similarity Assessment of ABP 710, a Biosimilar to Infliximab Reference Product.Pharmaceutical research · 2020Article
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- Rapid screening of IgG quality attributes - effects on Fc receptor binding.FEBS open bio · 2017Article
- AlphaScreen-based homogeneous assay using a pair of 25-residue artificial proteins for high-throughput analysis of non-native IgG.Scientific reports · 2017Article
- Main Quality Attributes of Monoclonal Antibodies and Effect of Cell Culture ComponentsIranian biomedical journal · 2017Review
- Characterization of mAb dimers reveals predominant dimer forms common in therapeutic mAbs.mAbs · 2016Article
- Quantifying Trace Amounts of Aggregates in Biopharmaceuticals Using Analytical Ultracentrifugation Sedimentation Velocity: Bayesian Analyses and F Statistics.The AAPS journal · 2016Article
- Comparative Evaluation of Two Methods for Preparative Fractionation of Proteinaceous Subvisible Particles--Differential Centrifugation and FACS.Pharmaceutical research · 2015Article
- The immunogenicity of antibody aggregates in a novel transgenic mouse model.Pharmaceutical research · 2015Article
- Article
- Direct analysis of mAb aggregates in mammalian cell culture supernatant.BMC biotechnology · 2014Article
- Aggregation mechanism of an IgG2 and two IgG1 monoclonal antibodies at low pH: from oligomers to larger aggregates.Pharmaceutical research · 2013Article
- Article
- Structural analysis of a therapeutic monoclonal antibody dimer by hydroxyl radical footprinting.mAbsArticle
- A comparison of biophysical characterization techniques in predicting monoclonal antibody stability.mAbsArticle
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeTo investigate structure and function of different monoclonal antibody (MAb) dimers.
methodsMAb dimers were induced by process-related, low pH and UV light stress. Dimers were isolated and purified by chromatography and extensively characterized by biochemical, structural and functional methods.
resultsHighly purified dimer forms were obtained which enabled detailed characterization. Dimers induced by process stress were associated by a single non-covalent interaction site between two Fab domains in a characteristic "bone-like" structure observed in Transmission Electron Microscopy (TEM). These dimers showed reduced potency and antigen binding affinity. Low pH stress generated more stable but also non-covalently associated dimers without chemical alterations in a typical "closed" conformation according to TEM. These dimer species were more compact and more hydrophobic as dimers induced by process stress. They showed bioactivity and antigen binding affinity similar to the native monomer. Light-induced dimers, exhibiting various different conformations, were the most stable dimers with various chemical modifications leading to a broad range in size, charge and hydrophobicity. These dimers fully lost bioactivity and antigen binding affinity.
conclusionThe use of highly purified MAb dimers and a panel of characterizations methods enabled to obtain a clear picture about molecular architecture and function of dimers.
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