ArticleScientific reports2017
Rapid and accurate in silico solubility screening of a monoclonal antibody library.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
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Who cites it
76 citing papers in PubMed, 140 citations in OpenAlex.
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- Control of Synaptic Communication through Molecularly Engineered Bioluminescence Light Emission and Sensing.bioRxiv : the preprint server for biology · 2025Article
- A novel bispecific antibody targeting TNF-α and IL-6 receptor as a potent immunotherapeutic agent for inflammation.Applied microbiology and biotechnology · 2025Article
- NanoDeNovo: De Novo Design of Anti-Poliovirus I Sabin Strain Nanobodies by Semi-Automated Computational Pipeline.International journal of molecular sciences · 2025Article
- Hinge Truncation to Improve Aggregation Kinetics and Thermal Stability of an Antibody Fab Fragment.Molecular pharmaceutics · 2025Article
- Enhancing the Protein Stability of an Anticancer VHH-Fc Heavy Chain Antibody through Computational Modeling and Variant Design.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Optimization of synthetic human VProtein science : a publication of the Protein Society · 2025Article
- Rationalizing mAb Candidate Screening Using a Single Holistic Developability Parameter.Molecular pharmaceutics · 2025Article
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- A novel peptide-based tau aggregation inhibitor as a potential therapeutic for Alzheimer's disease and other tauopathies.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024Article
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Automated optimization of the solubility of a hyper-stable α-amylase.Open biology · 2024Article
16 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibodies represent essential tools in research and diagnostics and are rapidly growing in importance as therapeutics. Commonly used methods to obtain novel antibodies typically yield several candidates capable of engaging a given target. The development steps that follow, however, are usually performed with only one or few candidates since they can be resource demanding, thereby increasing the risk of failure of the overall antibody discovery program. In particular, insufficient solubility, which may lead to aggregation under typical storage conditions, often hinders the ability of a candidate antibody to be developed and manufactured. Here we show that the selection of soluble lead antibodies from an initial library screening can be greatly facilitated by a fast computational prediction of solubility that requires only the amino acid sequence as input. We quantitatively validate this approach on a panel of nine distinct monoclonal antibodies targeting nerve growth factor (NGF), for which we compare the predicted and measured solubilities finding a very close match, and we further benchmark our predictions with published experimental data on aggregation hotspots and solubility of mutational variants of one of these antibodies.
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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.