ArticleBiophysical journal2014
Explaining the non-newtonian character of aggregating monoclonal antibody solutions using small-angle neutron scattering.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Article
- Enabling Efficient Design of Biological Formulations Through Advanced Characterization.Pharmaceutical research · 2023Review
- Using Cluster Theory to Calculate the Experimental Structure Factors of Antibody Solutions.Molecular pharmaceutics · 2023Article
- Analytical Techniques for the Characterization and Quantification of Monoclonal Antibodies.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Characterization of Monoclonal Antibody-Protein Antigen Complexes Using Small-Angle Scattering and Molecular Modeling.Antibodies (Basel, Switzerland) · 2017Article
- Critical examination of the colloidal particle model of globular proteins.Biophysical journal · 2015Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A monoclonal antibody solution displays an increase in low shear rate viscosity upon aggregation after prolonged incubation at 40°C. The morphology and interactions leading to the formation of the aggregates responsible for this non-Newtonian character are resolved using small-angle neutron scattering. Our data show a weak repulsive barrier before proteins aggregate reversibly, unless a favorable contact with high binding energy occurs. Two types of aggregates were identified after incubation at 40°C: oligomers with radius of gyration ∼10 nm and fractal submicrometer particles formed by a slow reaction-limited aggregation process, consistent with monomers colliding many times before finding a favorable strong interaction site. Before incubation, these antibody solutions are Newtonian liquids with no increase in low shear rate viscosity and no upturn in scattering at low wavevector, whereas aggregated solutions under the same conditions have both of these features. These results demonstrate that fractal submicrometer particles are responsible for the increase in low shear rate viscosity and low wavevector upturn in scattered intensity of aggregated antibody solutions; both are removed from aggregated samples by filtering.
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