ArticlemAbs
A fully synthetic human Fab antibody library based on fixed VH/VL framework pairings with favorable biophysical properties.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.
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Who cites it
108 citing papers in PubMed.
- Trial
- Article
- Antibody format matters: A comparative analysis of VHH and scFv domains reveals superior in vivo CAR T cell function with VHH domains.Molecular therapy : the journal of the American Society of Gene Therapy · 2026Article
- Fully human antagonistic antibodies targeting FPR2 through dual extracellular-loop engagement for gastric cancer therapy.Antibody therapeutics · 2026Article
- Elucidating the relationship between affinity and potency in the performance of therapeutic IgE.Scientific reports · 2026Article
- Phage Display Technology: Design, Library Construction, and Panning Strategies for Antibody Development.Biomolecules & therapeutics · 2026Review
- Long-range allosteric communication within antibodies affects antigen-binding affinity.Frontiers in immunology · 2026Article
- Article
- Pioneer: a synthetic human antibody phage display library for rapid therapeutic lead generation.mAbs · 2025Article
- Guidelines in the Preparation of Fully Synthetic, Human Single-Domain Antibody Phage Display Libraries.Antibodies (Basel, Switzerland) · 2025Article
- Design, Construction, and Validation of a Yeast-Displayed Chemically Expanded Antibody Library.ACS synthetic biology · 2025Article
- Discovery of Antibodies Against Endemic Coronaviruses with NGS-Based Human Fab Phage Display Platform.Antibodies (Basel, Switzerland) · 2025Article
- Identification of primary mediastinal B-cell lymphomas with higher clonal dominance and poorer outcome using 5'RACE.Blood advances · 2025Article
- A bispecific CD40 agonistic antibody allowing for antibody-peptide conjugate formation to enable cancer-specific peptide delivery, resulting in improved T proliferation and anti-tumor immunity in mice.Nature communications · 2024Article
- De novo protein sequencing of antibodies for identification of neutralizing antibodies in human plasma post SARS-CoV-2 vaccination.Nature communications · 2024Article
- Biophysical cartography of the native and human-engineered antibody landscapes quantifies the plasticity of antibody developability.Communications biology · 2024Article
- The rise of big data: deep sequencing-driven computational methods are transforming the landscape of synthetic antibody design.Journal of biomedical science · 2024Review
- Advancements in mammalian display technology for therapeutic antibody development and beyond: current landscape, challenges, and future prospects.Frontiers in immunology · 2024Review
- Comparative stability and analytical performance of anti-miroestrol recombinant antibody in different cassettes.Applied microbiology and biotechnology · 2023Article
- Development of a new recombinant antibody, selected by phage-display technology from a celiac patient library, for detection of gluten in foods.Current research in food science · 2023Article
48 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
17 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This report describes the design, generation and testing of Ylanthia, a fully synthetic human Fab antibody library with 1.3E+11 clones. Ylanthia comprises 36 fixed immunoglobulin (Ig) variable heavy (VH)/variable light (VL) chain pairs, which cover a broad range of canonical complementarity-determining region (CDR) structures. The variable Ig heavy and Ig light (VH/VL) chain pairs were selected for biophysical characteristics favorable to manufacturing and development. The selection process included multiple parameters, e.g., assessment of protein expression yield, thermal stability and aggregation propensity in fragment antigen binding (Fab) and IgG1 formats, and relative Fab display rate on phage. The framework regions are fixed and the diversified CDRs were designed based on a systematic analysis of a large set of rearranged human antibody sequences. Care was taken to minimize the occurrence of potential posttranslational modification sites within the CDRs. Phage selection was performed against various antigens and unique antibodies with excellent biophysical properties were isolated. Our results confirm that quality can be built into an antibody library by prudent selection of unmodified, fully human VH/VL pairs as scaffolds.
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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.