ArticlemAbs
Development of a high-throughput solubility screening assay for use in antibody discovery.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
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- Engineering HIV antibodies with enhanced breadth and potency of neutralization through multistate affinity maturation.bioRxiv : the preprint server for biology · 2025Article
- Barcoded screening identifies nanocarriers for protein delivery to kidney.Nature communications · 2025Article
- Sequence-based prediction of the intrinsic solubility of peptides containing non-natural amino acids.Nature communications · 2023Article
- Multidimensional Protein Solubility Optimization with an Ultrahigh-Throughput Microfluidic Platform.Analytical chemistry · 2023Article
- Accelerating therapeutic protein design with computational approaches toward the clinical stage.Computational and structural biotechnology journal · 2023Review
- Developability assessment at early-stage discovery to enable development of antibody-derived therapeutics.Antibody therapeutics · 2023Review
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- Assessment of Therapeutic Antibody Developability by Combinations of In Vitro and In Silico Methods.Methods in molecular biology (Clifton, N.J.) · 2022Article
- An open-source automated PEG precipitation assay to measure the relative solubility of proteins with low material requirement.Scientific reports · 2021Article
- Revisit PEG-Induced Precipitation Assay for Protein Solubility Assessment of Monoclonal Antibody Formulations.Pharmaceutical research · 2021Article
- High-throughput developability assays enable library-scale identification of producible protein scaffold variants.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Toward Drug-Like Multispecific Antibodies by Design.International journal of molecular sciences · 2020Review
- Electrostatic interactions modulate the differential aggregation propensities of IgG1 and IgG4P antibodies and inform charged residue substitutions for improved developability.Protein engineering, design & selection : PEDS · 2019Article
- Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Poor solubility is a common challenge encountered during the development of high concentration monoclonal antibody (mAb) formulations, but there are currently no methods that can provide predictive information on high-concentration behavior of mAbs in early discovery. We explored the utility of methodologies used for determining extrapolated solubility as a way to rank-order mAbs based on their relative solubility properties. We devised two approaches to accomplish this: 1) vapor diffusion technique utilized in traditional protein crystallization practice, and 2) polyethylene glycol (PEG)-induced precipitation and quantitation by turbidity. Using a variety of in-house mAbs with known high-concentration behavior, we demonstrated that both approaches exhibited reliable predictability of the relative solubility properties of these mAbs. Optimizing the latter approach, we developed a format that is capable of screening a large panel of mAbs in multiple pH and buffer conditions. This simple, material-saving, high-throughput approach enables the selection of superior molecules and optimal formulation conditions much earlier in the antibody discovery process, prior to time-consuming and material intensive high-concentration studies.
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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.