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

Sci Rep

July 2025

Advanced Diagnostics and Biomarker Discovery Research Team, National Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency (NSTDA), 111 Thailand Science Park, Phahonyothin Road, Pathum Thani, 12120, Thailand.

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.

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Detection and quantification of nanoplastic particles (NPs) in environmental water are important for monitoring NPs' fate and assessing health impacts, but the lack of sensitive and universal detection systems hinders regulation according to the EU Commission (Allan, J. et al., 2021).

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Background: Co-trimoxazole is a leading global cause of severe cutaneous adverse drug reactions (SCAR) including Stevens-Johnson syndrome/toxic epidermal necrolysis (SJS/TEN) and drug reaction with eosinophilia and systemic symptoms (DRESS). Co-trimoxazole-induced SCAR are associated with HLA class I alleles including HLA-B*13:01 and HLA-B*38:02 in Southeast Asian (SEA) populations. However, the global generalizability of these associations is unknown but critical for population-appropriate risk stratification and diagnosis.

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Since the outbreak of novel coronavirus pneumonia (COVID-19), numerous T-cell epitopes in severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) proteome have been reported. However, most of the identified CD8 T-cell epitopes have been restricted primarily by HLA-A allotypes. The epitopes restricted by HLA-B and HLA-C allotypes are limited.

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Pectinase, an enzyme primarily produced from , is essential in various industrial applications. However, the enzyme's functionality at high temperatures is challenging, restricting its effectiveness and potential uses. Therefore, the present study investigated the potential of peptide binding to enhance the thermal stability of pectinase.

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