ArticleScientific reports2021
An open-source automated PEG precipitation assay to measure the relative solubility of proteins with low material requirement.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed.
- Preventing physical and chemical degradation of the LABL-Fc-MOGAntibody therapeutics · 2026Article
- Rapid Development of High Concentration Protein Formulation Driven by High-Throughput Technologies.Pharmaceutical research · 2025Article
- Article
- Protein Precipitation by Metal Hydroxides as a Convenient and Alternative Sample Preparation Procedure for Bioanalysis.Molecules (Basel, Switzerland) · 2024Article
- Aggrescan4D: structure-informed analysis of pH-dependent protein aggregation.Nucleic acids research · 2024Article
- Automated optimization of the solubility of a hyper-stable α-amylase.Open biology · 2024Article
- Sequence-based prediction of the intrinsic solubility of peptides containing non-natural amino acids.Nature communications · 2023Article
- Automated optimisation of solubility and conformational stability of antibodies and proteins.Nature communications · 2023Article
- Multidimensional Protein Solubility Optimization with an Ultrahigh-Throughput Microfluidic Platform.Analytical chemistry · 2023Article
- Sequence-based prediction of pH-dependent protein solubility using CamSol.Briefings in bioinformatics · 2023Article
- Molecular Determinants of Fibrillation in a Viral Amyloidogenic Domain from Combined Biochemical and Biophysical Studies.International journal of molecular sciences · 2022Article
- Microfluidics for multiscale studies of biomolecular condensates.Lab on a chip · 2022Review
- Exposome, Molecular Pathways and One Health: The InvertebrateInternational journal of molecular sciences · 2022Review
- Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The solubility of proteins correlates with a variety of their properties, including function, production yield, pharmacokinetics, and formulation at high concentrations. High solubility is therefore a key requirement for the development of protein-based reagents for applications in life sciences, biotechnology, diagnostics, and therapeutics. Accurate solubility measurements, however, remain challenging and resource intensive, which limits their throughput and hence their applicability at the early stages of development pipelines, when long-lists of candidates are typically available in minute amounts. Here, we present an automated method based on the titration of a crowding agent (polyethylene glycol, PEG) to quantitatively assess relative solubility of proteins using about 200 µg of purified material. Our results demonstrate that this method is accurate and economical in material requirement and costs of reagents, which makes it suitable for high-throughput screening. This approach is freely-shared and based on a low cost, open-source liquid-handling robot. We anticipate that this method will facilitate the assessment of the developability of proteins and make it substantially more accessible.
Identifiers
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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.