# Exploiting and enhancing IgE-binding epitopes of the 2S albumins of peanuts and tree nuts

> **NIH NIH R01** · UNIVERSITY OF COLORADO DENVER · 2022 · $689,517

## Abstract

Abstract:
IgE-mediated food allergy to peanuts (PN) and/or tree nuts (TN), is a major health problem in
the United States, affecting approximately 4% of children and up to 2% of adults. Co-allergy
among these foods is relatively common and is difficult to identify given the more common
finding of co-sensitization. Recent progress with early administration of these foods and oral
immunotherapy, especially in conjunction with anti-IgE have merit. Unfortunately, these
approaches are not successful for all patients and, even when successful, have limitations
regarding compliance and unpredictable breakthrough. There are significant, unmet needs to
1) understand the immunologic details of IgE mediated activation of mast cells by allergens
from PN and TN, 2) understand the molecular basis for co-allergy among TN and between PN
and TN, 3) develop improved diagnostics to identify clinically relevant peanut and tree nut
allergy and 4) design new approaches to interfere with allergic reactions caused by peanuts.
The overarching concept of this proposal is that the 2S albumins are the most important
allergens of peanuts and tree nuts and are the key to understanding PN and TN allergy and
cross-reactivity and to developing potent diagnostic and potentially therapeutic reagents.
Preliminary data show that we have 1) developed a sensitive ELISA assay, 2) identified the
critical amino acids within IgE-binding peptides, 3) demonstrated that conformationally
constrained (3D) peptides bind IgE strongly and 4) shown that patients with PN allergy alone
and PN + TN allergy identify different patterns of peptides in a microarray assay. We
hypothesize that 1) we can optimize IgE binding to existing peptides and discover novel
peptides with enhanced binding, 2) there are cross- reacting epitopes of PN and selected TN
and 3) IgE binding to existing and novel peptides will have potential predictive value for
important clinical outcomes. We propose to 1) perform positional amino acid (aa) screening to
optimize binding of IgE to peptides, 2) utilize click chemistry and stapling technology to
enhance IgE binding and resistance to proteases and 3) use microarray technology to assess
IgE binding with well-defined samples from patients with PN, WN, PecN, CN and PisN allergy
and from those undergoing clinical trials. Success in this project will establish a new
intellectual framework regarding allergen/IgE interactions, describe, at least in part, the
molecular basis for these co-allergies, design new diagnostics and move us along the path
toward development of an oral, peptide based, treatment for peanut allergy.

## Key facts

- **NIH application ID:** 10490872
- **Project number:** 5R01AI165866-02
- **Recipient organization:** UNIVERSITY OF COLORADO DENVER
- **Principal Investigator:** STEPHEN C DRESKIN
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2022
- **Award amount:** $689,517
- **Award type:** 5
- **Project period:** 2021-09-17 → 2026-08-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10490872

## Citation

> US National Institutes of Health, RePORTER application 10490872, Exploiting and enhancing IgE-binding epitopes of the 2S albumins of peanuts and tree nuts (5R01AI165866-02). Retrieved via AI Analytics 2026-05-23 from https://api.ai-analytics.org/grant/nih/10490872. Licensed CC0.

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