ArticleBiophysical journal2010
Diffusion and sedimentation interaction parameters for measuring the second virial coefficient and their utility as predictors of protein aggregation.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed.
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- The origins of nonideality exhibited by monoclonal antibodies and Fab fragments in human serum.Protein science : a publication of the Protein Society · 2023Article
- On the utility of microfluidic systems to study protein interactions: advantages, challenges, and applications.European biophysics journal : EBJ · 2023Review
- In vitro measurement of concentration of unlabeled protein within a hyaluronic acid matrix.Biotechnology and bioengineering · 2022Article
- Effects of Monovalent Salt on Protein-Protein Interactions of Dilute and Concentrated Monoclonal Antibody Formulations.Antibodies (Basel, Switzerland) · 2022Article
- Measuring Self-Association of Antibody Lead Candidates with Dynamic Light Scattering.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Probing interactions of therapeutic antibodies with serum via second virial coefficient measurements.Biophysical journal · 2021Article
- Genetic modification to design a stable yeast-expressed recombinant SARS-CoV-2 receptor binding domain as a COVID-19 vaccine candidate.Biochimica et biophysica acta. General subjects · 2021Article
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Authors and funding
5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The concentration-dependence of the diffusion and sedimentation coefficients (k(D) and k(s), respectively) of a protein can be used to determine the second virial coefficient (B₂), a parameter valuable in predicting protein-protein interactions. Accurate measurement of B₂ under physiologically and pharmaceutically relevant conditions, however, requires independent measurement of k(D) and k(s) via orthogonal techniques. We demonstrate this by utilizing sedimentation velocity (SV) and dynamic light scattering (DLS) to analyze solutions of hen-egg white lysozyme (HEWL) and a monoclonal antibody (mAb1) in different salt solutions. The accuracy of the SV-DLS method was established by comparing measured and literature B₂ values for HEWL. In contrast to the assumptions necessary for determining k(D) and k(s) via SV alone, k(D) and ks were of comparable magnitudes, and solution conditions were noted for both HEWL and mAb1 under which 1), k(D) and k(s) assumed opposite signs; and 2), k(D) ≥k(s). Further, we demonstrate the utility of k(D) and k(s) as qualitative predictors of protein aggregation through agitation and accelerated stability studies. Aggregation of mAb1 correlated well with B₂, k(D), and k(s), thus establishing the potential for k(D) to serve as a high-throughput predictor of protein aggregation.
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