ArticlePharmaceutical research2011
Establishing a link between amino acid sequences and self-associating and viscoelastic behavior of two closely related monoclonal antibodies.
Article in Pharmaceutical research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 126 citations in OpenAlex.
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- The Relationship between Protein-Protein Interactions and Liquid-Liquid Phase Separation for Monoclonal Antibodies.Molecular pharmaceutics · 2023Article
- How can we discover developable antibody-based biotherapeutics?Frontiers in molecular biosciences · 2023Review
- Non-specificity as the sticky problem in therapeutic antibody development.Nature reviews. Chemistry · 2022Review
- Antibodies with Weakly Basic Isoelectric Points Minimize Trade-offs between Formulation and Physiological Colloidal Properties.Molecular pharmaceutics · 2022Article
- Utility of High Resolution 2D NMR Fingerprinting in Assessing Viscosity of Therapeutic Monoclonal Antibodies.Pharmaceutical research · 2022Article
- Selective Detection ofBiosensors · 2022Article
- Metal Ion Interactions with mAbs: Part 2. Zinc-Mediated Aggregation of IgG1 Monoclonal Antibodies.Pharmaceutical research · 2021Article
- A microfluidic approach to studying the injection flow of concentrated albumin solutions.SN applied sciences · 2021Article
- Analysis of nonideality: insights from high concentration simulations of sedimentation velocity data.European biophysics journal : EBJ · 2020Article
- Physicochemical Rules for Identifying Monoclonal Antibodies with Drug-like Specificity.Molecular pharmaceutics · 2020Article
- Multiscale Coarse-Grained Approach to Investigate Self-Association of Antibodies.Biophysical journal · 2020Article
- CLASP2 binding to curved microtubule tips promotes flux and stabilizes kinetochore attachments.The Journal of cell biology · 2020Article
- Impact of electroviscous effect on viscosity in developing highly concentrated protein formulations: Lessons from non-protein charged colloids.International journal of pharmaceutics: X · 2019Review
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeTo investigate the underlying cause for the observed differences in self-associating and viscoelastic behavior between two monoclonal antibodies, MAb1, and MAb2.
methodsSeveral mutants were designed by swapping charged residues in MAb1 with those present in MAb2 at their respective positions and vice versa. Rheological analysis was done at low and high shear rates. Dynamic light scattering quantified intermolecular interactions in dilute solutions; sedimentation equilibrium analysis determined the corrected weight average molecular weight (M (wc)) to assess the self-associating behavior in high concentration. The molecular charge was estimated from electrophoretic mobility measurements.
resultsReplacing the charged residues in the CDR of MAb1 resulted in a lower M (wc) and solution viscosity. The corresponding changes in either just the variable light (VL) or variable heavy (VH) chain showed only a partial decrease in viscosity, whereas changes in both VL and VH chains resulted in a dramatic reduction in viscosity. The converse case where the VL and VH chains of MAb2 were made to look like MAb1 did not self-associate or show increased viscosity.
conclusionsExposed charged residues in the CDR of MAb1 are critical in determining the self-associating and highly viscous behavior observed at high concentrations.
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