Identification of novel human IgE-binding peptides from a phage display library for total IgE detection

Abstract

Immunoglobulin E (IgE) plays a key role in allergic reactions and parasitic infections. Accurate detection of IgE is essential for the diagnosis and management of allergic diseases. Traditional detection methods, such as enzyme-linked immunosorbent assay (ELISA) and radioallergosorbent tests (RASTs), depend on complex antibody production processes. This study aimed to discover novel peptides that specifically bind to human IgE using phage display technology. A 12-mer phage-displayed peptide library was screened against native human IgE, resulting in the identification of sixteen high-specificity phage clones from an initial pool of 208 candidates. Six of these clones were selected for peptide synthesis and further evaluation using multiplex assays. All synthetic peptides demonstrated specific binding to human IgE, with no cross-reactivity observed against other human immunoglobulin isotypes (IgA, IgG, and IgM) or antibodies from other species (goat, mouse, and rat). Sensitivity analysis revealed that four peptides exhibited low detection limits, highlighting their potential for use in IgE quantification. This study is the first report synthetic peptides that specifically target human IgE. These peptides offer significant advantages over traditional antibody-based methods, including improved stability, simplicity, and cost-effectiveness. They represent promising candidates for developing new diagnostic tools for IgE detection. However, additional optimization and clinical validation are required to confirm their practical in diagnostic settings.