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Designer covalent heterobivalent inhibitors prevent IgE-dependent responses to peanut allergen
Open accessAbstract
Significance: IgE antibody interaction with allergen proteins is the main driver for life-threating allergic responses. Using a nanoparticle-based method, we identified the most crucial binding sites for IgEs on peanut proteins by testing a small population of patient serum with a clinical history of severe allergies to peanuts. We then synthesized inhibitors, we call covalent heterobivalent inhibitors, which specifically and permanently prevent IgEs from binding to peanut proteins and triggering allergic responses. This is significant as it seems that only a few binding sites on peanut allergen proteins drive allergic responses. Also, this is a functional example of selective IgE inhibition to a relevant food allergen and establishes cHBIs as a class of allergy therapeutics.
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In the specific field of oncology, one covalent PPI inhibitor has been approved by the FDA, while others have entered clinical trials.
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Metadata
- Authors
- Deak, P. E., Kim, B., Abdul Qayum, A., Shin, J., Vitalpur, G., Kloepfer, K. M., Turner, M. J., Smith, N., Shreffler, W. G., Kiziltepe, T., Kaplan, M. H., & Bilgicer, B.
- Affiliations
- University of Notre Dame (US)
- Department of Pediatrics, Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202;
- Department of Chemical and Biomolecular Engineering, University of Notre Dame, Notre Dame, IN 46556;
- Riley Hospital for Children (US)
- Richard L. Roudebush VA Medical Center (US)
- Massachusetts General Hospital (US)
- Indiana University Indianapolis (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2019-04-08
- Volume
- 116
- Issue
- 18
- Pages
- 8966-8974
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC6500160
- OpenAlex
- W2936094186
- Cited by
- 20
- References
- 39
- Citations by year
- 2026: 1 · 2024: 5 · 2023: 5 · 2022: 2 · 2021: 3 · 2020: 3 · 2019: 1
- FWCI
- 1.71
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- IUScholarWorks (Indiana University) (submittedVersion)
- PMC
- Funders
- Division of Intramural Research, National Institute of Allergy and Infectious Diseases (R01AI108884, R01AI129241, U19 AI095261, T32 DK007519)
- Center for Integrated Healthcare, U.S. Department of Veterans Affairs (IK2 CX001019)
- IU Simon Cancer Center (P30 CA082709, U54 DK106846)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Food Allergy and Anaphylaxis Research
- Health Sciences › Medicine › Immunology and Allergy › Allergic Rhinitis and Sensitization
- Life Sciences › Immunology and Microbiology › Immunology › Mast cells and histamine
- Keywords
- peanut allergy, specific IgE, immunodominant epitopes, basophil activation, mast cells, food allergy, epitope mapping
- MeSH terms
- Allergens, Epitopes, Basophils, Humans, Hypersensitivity, Immunoglobulin E, Mast Cells, Arachis, Cell Degranulation, Peanut Hypersensitivity, Galectin 3, Nanoparticles
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