ArticleScientific reports2021
Size-based characterization of adalimumab and TNF-α interactions using flow induced dispersion analysis: assessment of avidity-stabilized multiple bound species.
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.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Microfluidics for protein interaction studies: current methods, challenges, and future perspectives.European biophysics journal : EBJ · 2026Review
- Flow-induced dispersion analysis for probing cyclodextrin-guest binding interactions.European biophysics journal : EBJ · 2026Article
- Lignin Molar Mass Estimation by Dispersion Analysis.Macromolecular rapid communications · 2025Article
- Article
- Infliximab in Inflammatory Bowel Disease: Leveraging Physiologically Based Pharmacokinetic Modeling in the Clinical Context.Biomedicines · 2024Article
- Molecular properties and diagnostic potential of monoclonal antibodies targeting cytotoxic α-synuclein oligomers.NPJ Parkinson's disease · 2024Article
- Microgels as Platforms for Antibody-Mediated Cytokine Scavenging.Advanced healthcare materials · 2023Article
- Protein Binding: A Fuzzy Concept.Life (Basel, Switzerland) · 2023Article
- Antigen footprint governs activation of the B cell receptor.Nature communications · 2023Article
- Immobilization-Free Binding and Affinity Characterization of Higher Order Bispecific Antibody Complexes Using Size-Based Microfluidics.Analytical chemistry · 2022Article
- Quantification of Structural Integrity and Stability Using Nanograms of Protein by Flow-Induced Dispersion Analysis.Molecules (Basel, Switzerland) · 2022Article
- Assessment of immunogenicity and drug activity in patient sera by flow-induced dispersion analysis.Scientific reports · 2022Article
- HLAII peptide presentation of infliximab increases when complexed with TNF.Frontiers in immunology · 2022Article
- Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The understanding and characterization of protein interactions is crucial for elucidation of complicated biomolecular processes as well as for the development of new biopharmaceutical therapies. Often, protein interactions involve multiple binding, avidity, oligomerization, and are dependent on the local environment. Current analytical methodologies are unable to provide a detailed mechanistic characterization considering all these parameters, since they often rely on surface immobilization, cannot measure under biorelevant conditions, or do not feature a structurally-related readout for indicating formation of multiple bound species. In this work, we report the use of flow induced dispersion analysis (FIDA) for in-solution characterization of complex protein interactions under in vivo like conditions. FIDA is an immobilization-free ligand binding methodology employing Taylor dispersion analysis for measuring the hydrodynamic radius (size) of biomolecular complexes. Here, the FIDA technology is utilized for a size-based characterization of the interaction between TNF-α and adalimumab. We report concentration-dependent complex sizes, binding affinities (K
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