ArticleComputational and structural biotechnology journal2025
Replacement of a single residue in an antibody abolishes cognate antigen binding, as predicted by theoretical methods.
Article in Computational and structural biotechnology journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- A Reversible ATR-FTIR Biosensor with Single-Residue Sensitivity.Analytical chemistry · 2026Article
- D81 Mutants Reveal Hidden EF-Tu Diversity while Natural Sequences Preserve Aspartate.Computational and structural biotechnology journal · 2026Article
- Revisiting the Ofatumumab Epitope on CD20 through Integrative Molecular Dynamics and Flow Cytometry Analyses.Computational and structural biotechnology journal · 2026Article
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Authors and funding
8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Structural insights into the interaction between antibodies and antigens at the atomic level are pivotal for understanding the molecular mechanisms of antigen binding. Despite the availability of structural models generated by recent artificial intelligence advancements, computational predictions require experimental validation to confirm their accuracy. Here, we demonstrate an approach that combines computational protein modeling with spectroscopic experiments to validate antibody-antigen interactions. As a case example we use solanezumab, a monoclonal antibody that targets amyloid-beta (Aβ), whose misfolding is the main factor responsible for Alzheimer's disease. For this antibody, we predicted a single mutation, G95A
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