Innovations in protein engineering can help redesign allergenic proteins to reduce adverse reactions in sensitive individuals. To accomplish this aim, a better knowledge of the molecular properties of allergenic proteins and the molecular features that make a protein allergenic is needed. We present a novel AI-based tool, AllergenAI, to quantify the allergenic potential of a given protein.
View Article and Find Full Text PDFThe deterministic preparation of highly ordered single-crystalline surfaces is a key step for studying and utilizing the physical properties of various advanced materials. This paper presents the fast and straightforward preparation of vicinal AlO(0001) surfaces with micrometer-scale atomic order. Crisp electron-diffraction spots up to at least 20 order evidence atomic coherence on terraces with widths exceeding 1 μm.
View Article and Find Full Text PDFBackground: Allergenic proteins can cause IgE-mediated adverse reactions in sensitized individuals. Although the sequences of many allergenic proteins have been identified, bioinformatics data analysis with advanced computational methods and modeling is needed to identify the basis for IgE binding and cross-reactivity.
Objective: We aim to present the features and use of the updated Structural Database of Allergenic Proteins 2.
Scope: The unstructured region of Ara h 2, referred to as epitope 3, contains a repeated motif, DYPSh (h = hydroxyproline) that is important for IgE binding.
Methods And Results: IgE binding assays to 20mer and shorter peptides of epitope 3, defines a 16mer core sequence containing one copy of the DPYSh motif, DEDSYERDPYShSQDP. This study performs alanine scanning of this and a related 12mer mimotope, LLDPYAhRAWTK.