ArticleThe journal of physical chemistry. B2021
Electrostatics Drive Oligomerization and Aggregation of Human Interferon Alpha-2a.
Article in The journal of physical chemistry. B, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Synthetic T-Cell Receptor-like Protein Behaves as a Janus Particle in Solution.Journal of the American Chemical Society · 2025Article
- Collection of serum albumin aggregate nanoparticles from human plasma by dielectrophoresis.Electrophoresis · 2024Article
- A multi-scale numerical approach to study monoclonal antibodies in solution.APL bioengineering · 2024Article
- Controlling the Quality of Nanodrugs According to Their New Property-Radiothermal Emission.Pharmaceutics · 2024Article
- Bovine Serum Albumin Rejection by an Open Ultrafiltration Membrane: Characterization and Modeling.Membranes · 2024Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aggregation is a common phenomenon in the field of protein therapeutics and can lead to function loss or immunogenic patient responses. Two strategies are currently used to reduce aggregation: (1) finding a suitable formulation, which is labor-intensive and requires large protein quantities, or (2) engineering the protein, which requires extensive knowledge about the protein aggregation pathway. We present a biophysical characterization of the oligomerization and aggregation processes by Interferon alpha-2a (IFNα-2a), a protein drug with antiviral and immunomodulatory properties. This study combines experimental high throughput screening with detailed investigations by small-angle X-ray scattering and analytical ultracentrifugation. Metropolis Monte Carlo simulations are used to gain insight into the underlying intermolecular interactions. IFNα-2a forms soluble oligomers that are controlled by a fast pH and concentration-dependent equilibrium. Close to the isoelectric point of 6, IFNα-2a forms insoluble aggregates which can be prevented by adding salt. We show that monomer
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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.