ArticleBiochemistry and biophysics reports2018
Improvement of antibody affinity by introduction of basic amino acid residues into the framework region.
Article in Biochemistry and biophysics reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Targeted drug conjugates and molecular mechanisms in overcoming lung cancer drug resistance.Discover oncology · 2025Review
- Antibody-drug conjugates as immuno-oncology agents in colorectal cancer: targets, payloads, and therapeutic synergies.Frontiers in immunology · 2025Review
- Drug conjugates for the treatment of lung cancer: from drug discovery to clinical practice.Experimental hematology & oncology · 2024Review
- Arginine cluster introduction on framework region in anti-lysozyme antibody improved association rate constant by changing conformational diversity of CDR loops.Protein science : a publication of the Protein Society · 2023Article
- Structure-Based Affinity Maturation of Antibody Based on Double-Point Mutations.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Antibody drug conjugate: the "biological missile" for targeted cancer therapy.Signal transduction and targeted therapy · 2022Review
- Improvement of the affinity of an anti-rat P2X4 receptor antibody by introducing electrostatic interactions.Scientific reports · 2022Article
- Fast-dissociating but highly specific antibodies are novel tools in biology, especially useful for multiplex super-resolution microscopy.STAR protocols · 2021Article
- Plasmonic photothermal release of docetaxel by gold nanoparticles incorporated onto halloysite nanotubes with conjugated 2D8-E3 antibodies for selective cancer therapy.Journal of nanobiotechnology · 2021Article
- Article
- Semi-automated single-molecule microscopy screening of fast-dissociating specific antibodies directly from hybridoma cultures.Cell reports · 2021Article
- Structure-based design and discovery of novel anti-tissue factor antibodies with cooperative double-point mutations, using interaction analysis.Scientific reports · 2020Article
- Natural Catalytic IgGs Hydrolyzing Histones in Schizophrenia: Are They the Link between Humoral Immunity and Inflammation?International journal of molecular sciences · 2020Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibodies are widely used not only as therapeutic agents but also as research tools and diagnostic agents, and extensive efforts have been made to generate antibodies that have higher affinity. It was recently reported that introduction of charged residues into the framework region of an antibody improved its affinity; however, the underlying molecular mechanism has not been elucidated. In this study, we used kinetic and thermodynamic analyses of the antibody-antigen interaction to investigate the molecular mechanism by which an antibody with introduced charged residues recognizes its antigen with higher affinity. The introduction of basic amino acid residues resulted in improvement of the affinity whereas the introduction of acidic residues weakened the interaction. For two mutant antigen-binding fragments (Fabs) with improved affinity (named K5- and R5-mutants), the balance between the association rate constant
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