ArticleProceedings of the National Academy of Sciences of the United States of America2013
Identification and grafting of a unique peptide-binding site in the Fab framework of monoclonal antibodies.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
32 citing papers in PubMed, 52 citations in OpenAlex.
- Meditope-Enabled Chimeric Antigen Receptors Facilitate Plug-and-Play Control of T Cells.Cancer immunology research · 2026Article
- The Current Landscape of Modular CAR T Cells.International journal of molecular sciences · 2025Review
- Article
- Engineering of an Fc-specific monovalent protein G for the light-controlled affinity purification of antibodies.Scientific reports · 2025Article
- Thermostability and binding properties of single-chained Fv fragments derived from therapeutic antibodies.Protein science : a publication of the Protein Society · 2024Article
- A disruptive clickable antibody design for the generation of antibody-drug conjugates.Antibody therapeutics · 2023Article
- Using quantitative single molecule localization microscopy to optimize multivalent HER2-targeting ligands.Frontiers in medicine · 2023Article
- Antibody-based redirection of universal Fabrack-CAR T cells selectively kill antigen bearing tumor cells.Journal for immunotherapy of cancer · 2022Article
- Synthesis of Multi-Protein Complexes through Charge-Directed Sequential Activation of Tyrosine Residues.Journal of the American Chemical Society · 2021Article
- Article
- Non-covalent albumin-binding ligands for extending the circulating half-life of small biotherapeutics.MedChemComm · 2019Review
- Refining the Quality of Monoclonal Antibodies: Grafting Unique Peptide-Binding Site in the Fab Framework.Methods in molecular biology (Clifton, N.J.) · 2019Article
- A Platform To Enhance Quantitative Single Molecule Localization Microscopy.Journal of the American Chemical Society · 2018Article
- Template-Catalyzed, Disulfide Conjugation of Monoclonal Antibodies Using a Natural Amino Acid Tag.Bioconjugate chemistry · 2018Article
- Mechanically interlocked functionalization of monoclonal antibodies.Nature communications · 2018Article
- Dual-Color Bioluminescent Sensor Proteins for Therapeutic Drug Monitoring of Antitumor Antibodies.Analytical chemistry · 2018Article
- Meditope-Fab interaction: threading the hole.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Improving theranostics in pancreatic cancer.Journal of surgical oncology · 2017Review
- Engineering a high-affinity peptide binding site into the anti-CEA mAb M5A.Protein engineering, design & selection : PEDS · 2017Article
- Affinity Maturation of a Cyclic Peptide Handle for Therapeutic Antibodies Using Deep Mutational Scanning.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
Capitalizing on their extraordinary specificity, monoclonal antibodies (mAbs) have become one of the most reengineered classes of biological molecules. A major goal in many of these engineering efforts is to add new functionality to the parental mAb, including the addition of cytotoxins and imaging agents for medical applications. Herein, we present a unique peptide-binding site within the central cavity of the fragment antigen binding framework region of the chimeric, anti-epidermal growth factor receptor mAb cetuximab. We demonstrate through diffraction methods, biophysical studies, and sequence analysis that this peptide, a meditope, has moderate affinity for the Fab, is specific to cetuximab (i.e., does not bind to human IgGs), and has no significant effect on antigen binding. We further demonstrate by diffraction studies and biophysical methods that the meditope binding site can be grafted onto the anti-human epidermal growth factor receptor 2 mAb trastuzumab, and that the antigen binding affinity of the grafted trastuzumab is indistinguishable from the parental mAb. Finally, we demonstrate a bivalent meditope variant binds specifically and stably to antigen-bearing cells only in the presence of the meditope-enabled mAbs. Collectively, this finding and the subsequent characterization and engineering efforts indicate that this unique interface could serve as a noncovalent "linker" for any meditope-enabled mAb with applications in multiple mAb-based technologies including diagnostics, imaging, and therapeutic delivery.
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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.