ArticleProtein engineering, design & selection : PEDS2015
A fully human scFv phage display library for rapid antibody fragment reformatting.
Article in Protein engineering, design & selection : PEDS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- A Picomolar MBP-Binding Nanobody for Target Enrichment and Modular Complex Engineering.ACS bio & med chem Au · 2026Article
- A Paradigm Shift in Snakebite Envenoming Therapy: From Conventional Antivenoms to Rationally Designed, Broadly Neutralizing Combination Therapies.ACS pharmacology & translational science · 2026Review
- Integrated scFv identification and CAR T cell generation for AML targeting in vivo.International journal of cancer · 2026Article
- Single-Stranded Variable Fragment Gene Libraries Built for Phage Display: An Updated Review of Design, Selection and Application.Journal of microbiology and biotechnology · 2024Review
- Chimeric Protein Switch Biosensors.Advances in biochemical engineering/biotechnology · 2024Review
- Dual-inhibitory domain iCARs improve the efficiency of the AND-NOT gate CAR T strategy.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Development of an Antigen-Antibody Co-Display System for Detecting Interaction of G-Protein-Coupled Receptors and Single-Chain Variable Fragments.International journal of molecular sciences · 2021Article
- Nanobodies targeting immune checkpoint molecules for tumor immunotherapy and immunoimaging (Review).International journal of molecular medicine · 2021Review
- Golden Gate assembly with a bi-directional promoter (GBid): A simple, scalable method for phage display Fab library creation.Scientific reports · 2020Article
- Cognizance of Molecular Methods for the Generation of Mutagenic Phage Display Antibody Libraries for Affinity Maturation.International journal of molecular sciences · 2019Review
- Systemic surfaceome profiling identifies target antigens for immune-based therapy in subtypes of advanced prostate cancer.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- High-Throughput Approaches to the Development of Molecular Imaging Agents.Molecular imaging and biology · 2017Review
- Cell growth inhibition and apoptotic effects of a specific anti-RTFscFv antibody on prostate cancer, but not glioblastoma, cells.F1000Research · 2017Article
- An Effective Immuno-PET Imaging Method to Monitor CD8-Dependent Responses to Immunotherapy.Cancer research · 2016Article
- In Vitro Selection of Cancer Cell-Specific Molecular Recognition Elements from Amino Acid Libraries.Journal of immunology research · 2015Review
- Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
Phage display libraries of human single-chain variable fragments (scFvs) are a reliable source of fully human antibodies for scientific and clinical applications. Frequently, scFvs form the basis of larger, bivalent formats to increase valency and avidity. A small and versatile bivalent antibody fragment is the diabody, a cross-paired scFv dimer (∼55 kDa). However, generation of diabodies from selected scFvs requires decreasing the length of the interdomain scFv linker, typically by overlap PCR. To simplify this process, we designed two scFv linkers with integrated restriction sites for easy linker length reduction (17-residue to 7-residue or 18-residue to 5-residue, respectively) and generated two fully human scFv phage display libraries. The larger library (9 × 10(9) functional members) was employed for selection against a model antigen, human N-cadherin, yielding novel scFv clones with low nanomolar monovalent affinities. ScFv clones from both libraries were reformatted into diabodies by restriction enzyme digestion and re-ligation. Size-exclusion chromatography analysis confirmed the proper dimerization of most of the diabodies. In conclusion, these specially designed scFv phage display libraries allow us to rapidly reformat the selected scFvs into diabodies, which can greatly accelerate early stage antibody development when bivalent fragments are needed for candidate screening.
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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.