ArticleFrontiers in immunology2017
Facile Affinity Maturation of Antibody Variable Domains Using Natural Diversity Mutagenesis.
Article in Frontiers in immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
34 citing papers in PubMed.
- Computational nanobody design using graph neural networks and Metropolis Monte Carlo sampling.Briefings in bioinformatics · 2026Article
- Targeted inhibition of M2 macrophages polarization via a PDC attenuates chronic pancreatitis through the PPARα pathway.iScience · 2026Article
- Diagnosis of gout using monosodium urate (MSU) crystal binding peptides screened from Fv-antibody library.Analytical and bioanalytical chemistry · 2026Article
- Simultaneous Affinity Maturation and Liability Removal from Antibodies.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Single-Domain Antibodies That Specifically Recognize Intact Capsids of Multiple Foot-and-Mouth Disease Serotype O Strains.Vaccines · 2025Article
- Optimization of synthetic human VProtein science : a publication of the Protein Society · 2025Article
- Viral escape-inspired framework for structure-guided dual bait protein biosensor design.PLoS computational biology · 2025Article
- Surface patches induce nonspecific binding and phase separation of antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- How can we discover developable antibody-based biotherapeutics?Frontiers in molecular biosciences · 2023Review
- Non-specificity as the sticky problem in therapeutic antibody development.Nature reviews. Chemistry · 2022Review
- Article
- Immunoglobulin somatic hypermutation in a defined biochemical system recapitulates affinity maturation and permits antibody optimization.Nucleic acids research · 2022Article
- Research progress on unique paratope structure, antigen binding modes, and systematic mutagenesis strategies of single-domain antibodies.Frontiers in immunology · 2022Review
- Isolating Anti-amyloid Antibodies from Yeast-Displayed Libraries.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Affinity maturation: highlights in the application of in vitro strategies for the directed evolution of antibodies.Emerging topics in life sciences · 2021Article
- Peptide barcoding for one-pot evaluation of sequence-function relationships of nanobodies.Scientific reports · 2021Article
- ssDNA recombineering boosts in vivo evolution of nanobodies displayed on bacterial surfaces.Communications biology · 2021Article
- Syngeneic homograft of framework regions enhances the affinity of the mouse anti-human epidermal receptor 2 single-chain antibody e23sFv.Experimental and therapeutic medicine · 2021Article
- Exploring cellular biochemistry with nanobodies.The Journal of biological chemistry · 2020Review
- Structure-based design and discovery of novel anti-tissue factor antibodies with cooperative double-point mutations, using interaction analysis.Scientific reports · 2020Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The identification of mutations that enhance antibody affinity while maintaining high antibody specificity and stability is a time-consuming and laborious process. Here, we report an efficient methodology for systematically and rapidly enhancing the affinity of antibody variable domains while maximizing specificity and stability using novel synthetic antibody libraries. Our approach first uses computational and experimental alanine scanning mutagenesis to identify sites in the complementarity-determining regions (CDRs) that are permissive to mutagenesis while maintaining antigen binding. Next, we mutagenize the most permissive CDR positions using degenerate codons to encode wild-type residues and a small number of the most frequently occurring residues at each CDR position based on natural antibody diversity. This mutagenesis approach results in antibody libraries with variants that have a wide range of numbers of CDR mutations, including antibody domains with single mutations and others with tens of mutations. Finally, we sort the modest size libraries (~10 million variants) displayed on the surface of yeast to identify CDR mutations with the greatest increases in affinity. Importantly, we find that single-domain (V
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