ArticleNature communications2018
Measuring macromolecular size distributions and interactions at high concentrations by sedimentation velocity.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
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- Is there reversible dimerization of albumin in blood plasma? And does it matter?Experimental physiology · 2024Review
- BASIS: BioAnalysis SEDFIT integrated software for cGMP analysis of SV-AUC data.European biophysics journal : EBJ · 2024Article
- An automated interface for sedimentation velocity analysis in SEDFIT.PLoS computational biology · 2023Article
- Simulation of Gilbert theory for self-association in sedimentation velocity experiments: a guide to evaluate best fitting models.European biophysics journal : EBJ · 2023Article
- Retrospective rationalization of disparities between the concentration dependence of diffusion coefficients obtained by boundary spreading and dynamic light scattering.European biophysics journal : EBJ · 2023Article
- An automated interface for sedimentation velocity analysis in SEDFIT.bioRxiv : the preprint server for biology · 2023Article
- Insights into the biochemical and biophysical mechanisms mediating the longevity of the transparent optics of the eye lens.The Journal of biological chemistry · 2022Review
- Best Practices for Aggregate Quantitation of Antibody Therapeutics by Sedimentation Velocity Analytical Ultracentrifugation.Journal of pharmaceutical sciences · 2022Review
- Probing interactions of therapeutic antibodies with serum via second virial coefficient measurements.Biophysical journal · 2021Article
- Label-free methods for opticalPhysical chemistry chemical physics : PCCP · 2021Review
- Modification of cell wall polysaccharide guides cell division in Streptococcus mutans.Nature chemical biology · 2021Article
- A multi-step nucleation process determines the kinetics of prion-like domain phase separation.Nature communications · 2021Article
- Quantifying the concentration dependence of sedimentation coefficients for globular macromolecules: a continuing age-old problem.Biophysical reviews · 2021Review
- Global multi-method analysis of interaction parameters for reversibly self-associating macromolecules at high concentrations.Scientific reports · 2021Article
- Elucidation of the mechanism of subunit exchange in αB crystallin oligomers.Scientific reports · 2021Article
- Structurally plastic NEMO and oligomerization prone IKK2 subunits define the behavior of human IKK2:NEMO complexes in solution.Biochimica et biophysica acta. Proteins and proteomics · 2020Article
- Analysis of nonideality: insights from high concentration simulations of sedimentation velocity data.European biophysics journal : EBJ · 2020Article
- Sedimentation Velocity Analytical Ultracentrifugation Analysis of Marketed Rituximab Drug Product Size Distribution.Pharmaceutical research · 2020Article
- Resuspending samples in analytical ultracentrifugation.Analytical biochemistry · 2020Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
In concentrated macromolecular solutions, weak physical interactions control the solution behavior including particle size distribution, aggregation, liquid-liquid phase separation, or crystallization. This is central to many fields ranging from colloid chemistry to cell biology and pharmaceutical protein engineering. Unfortunately, it is very difficult to determine macromolecular assembly states and polydispersity at high concentrations in solution, since all motion is coupled through long-range hydrodynamic, electrostatic, steric, and other interactions, and scattering techniques report on the solution structure when average interparticle distances are comparable to macromolecular dimensions. Here we present a sedimentation velocity technique that, for the first time, can resolve macromolecular size distributions at high concentrations, by simultaneously accounting for average mutual hydrodynamic and thermodynamic interactions. It offers high resolution and sensitivity of protein solutions up to 50 mg/ml, extending studies of macromolecular solution state closer to the concentration range of therapeutic formulations, serum, or intracellular conditions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.