ArticleBiomacromolecules2020
Characterization and Control of Dynamic Rearrangement in a Self-Assembled Antibody Carrier.
Article in Biomacromolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Dual-function thermoresponsive antibiotic-loaded hydrogel with antimicrobial and osteogenic properties for implant-related infection control.Bioactive materials · 2026Article
- Engineering a Coiled-Coil Protein for DARPin Presentation as a Potent SARS-CoV-2 Therapeutic.Biomacromolecules · 2025Article
- Article
- Multi-Detection Size Exclusion Chromatography as an Advanced Tool for Monitoring Enzyme-Antibody Conjugation Reaction and Quality Control of a Final Product.Molecules (Basel, Switzerland) · 2023Article
- Coiled coil exposure and histidine tags drive function of an intracellular protein drug carrier.Journal of controlled release : official journal of the Controlled Release Society · 2021Article
- Supramolecular "Click Chemistry" for Targeting in the Body.Bioconjugate chemistry · 2021Review
- Antibody Nanocarriers for Cancer Management.Current opinion in biomedical engineering · 2021Article
- Demonstration of intracellular trafficking, cytosolic bioavailability, and target manipulation of an antibody delivery platform.Nanomedicine : nanotechnology, biology, and medicine · 2021Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Thorough characterization of protein assemblies is required for the control of structure and robust performance in any given application, especially for the safety and stability of protein therapeutics. Here, we report the use of multiple, orthogonal characterization techniques to enable control over the structure of a multivalent antibody carrier for future use in drug delivery applications. The carrier, known as Hex, contains six antibody binding domains that bind the Fc region of antibodies. Using size exclusion chromatography, analytical ultracentrifugation, and dynamic light scattering, we identified the stoichiometry of assembled Hex-antibody complexes and observed changes in the stoichiometry of nanocarriers when incubated at higher temperatures over time. The characterization data informed the modification of Hex to achieve tighter control over the protein assembly structure for future therapeutic applications. This work demonstrates the importance of using orthogonal characterization techniques and observing protein assembly in different conditions over time to fully understand and control structure and dynamics.
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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.