Predicting antibody developability profiles through early stage discovery screening
Open accessAbstract
Monoclonal antibodies play an increasingly important role for the development of new drugs across multiple therapy areas. The term 'developability' encompasses the feasibility of molecules to successfully progress from discovery to development via evaluation of their physicochemical properties. These properties include the tendency for self-interaction and aggregation, thermal stability, colloidal stability, and optimization of their properties through sequence engineering. Selection of the best antibody molecule based on biological function, efficacy, safety, and developability allows for a streamlined and successful CMC phase. An efficient and practical high-throughput developability workflow (100 s-1,000 s of molecules) implemented during early antibody generation and screening is crucial to select the best lead candidates. This involves careful assessment of critical developability parameters, combined with binding affinity and biological properties evaluation using small amounts of purified material (<1 mg), as well as an efficient data management and database system. Herein, a panel of 152 various human or humanized monoclonal antibodies was analyzed in biophysical property assays. Correlations between assays for different sets of properties were established. We demonstrated in two case studies that physicochemical properties and key assay endpoints correlate with key downstream process parameters. The workflow allows the elimination of antibodies with suboptimal properties and a rank ordering of molecules for further evaluation early in the candidate selection process. This enables any further engineering for problematic sequence attributes without affecting program timelines.
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Aggregation of antibody therapeutics can lead to precipitation and shortened storage period of drugs before administration, while aggregation in vivo can increase the immunogenicity of the drug.
“Aggregation of antibody therapeutics can lead to precipitation and shortened storage period of drugs before administration, while aggregation in vivo can increase the immunogenicity of the drug [22].”
From Computational and artificial intelligence-based methods for antibody development (2023) · cites this paper as [22]
In general, the developability of an antibody can be mostly predicted by physicochemical properties of the amino acid sequence, such as hydrophobicity, electrostatic charge, and the interaction in their topology pattern.
“In general, the developability of an antibody can be mostly predicted by physicochemical properties of the amino acid sequence, such as hydrophobicity, electrostatic charge, and the interaction in their topology pattern [22].”
From Computational and artificial intelligence-based methods for antibody development (2023) · cites this paper as [22]
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- Authors
- Bailly, M., Mieczkowski, C., Juan, V., Metwally, E., Tomazela, D., Baker, J., Uchida, M., Kofman, E., Raoufi, F., Motlagh, S., Yu, Y., Park, J., Raghava, S., Welsh, J., Rauscher, M., Raghunathan, G., Hsieh, M., Chen, Y.-L., Nguyen, H. T., Nguyen, N., Cipriano, D., & Fayadat-Dilman, L.
- Affiliations
- Protein Sciences
- Computation and Structural Chemistry, South San Francisco, CA, USA
- Pharmaceutical Sciences, Sterile FormulationSciences, Kenilworth, NJ, USA
- Downstream Process Development andEngineering, Kenilworth, NJ, USA
- ORCID
- Venue
- mAbs
- Publisher
- Informa UK Limited
- Published
- 2020-01
- Volume
- 12
- Issue
- 1
- Pages
- 1743053-1743053
- ISSN
- 1942-0862 (ISSN-L)
- 1942-0870
- PMC
- PMC7153844
- OpenAlex
- W3014709736
- Cited by
- 228
- References
- 80
- Citations by year
- 2026: 35 · 2025: 39 · 2024: 47 · 2023: 40 · 2022: 33 · 2021: 25 · 2020: 9
- FWCI
- 13.03
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- mAbs (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Immunology and Microbiology › Immunology › Biosimilars and Bioanalytical Methods
- Keywords
- monoclonal antibodies, developability, antibody aggregation, thermal stability, colloidal stability, physicochemical properties, binding affinity, humanized monoclonal antibody, candidate selection, sequence engineering
- MeSH terms
- Antibodies, Monoclonal, Humans, Protein Engineering, Drug Discovery, Workflow
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