Screening of prospective anti-allergic compounds as a common inhibitor for different proteinaceous allergens from animal

Abstract Exposure to protein-based allergens poses a growing health risk for individuals of all age groups. Already anti-allergy medications are commonly prescribed to reduce symptoms and inflammation. Allergen-specific common inhibitors against a wide spectrum of allergens may be applied to treatment. The aim of our study was to identify structurally homologous pockets present across various protein allergens and, using a similarity index, to identify for potential anti-allergic compounds that can target animal allergens. We collected and analysed a substantial dataset of a total of 62 proteinaceous allergen sequences and structures from animals. The effectiveness of 51 potential anti-allergic compounds was assessed through ADMET studies followed by high-throughput molecular docking. The AutoDock software was used to calculate the binding energies of these compounds, which helped identify the binding sites between proteinaceous allergens and potential anti-allergic agents. Further analysis of intra- and inter-sequence relationships, alongside structural examinations, showed notable structural similarities among the proteinaceous allergens of animals. Interatomic profiles of the compounds with allergens, Albiflorin and Paeoniflorigenone demonstrated the highest binding free energy (ΔG − 6.2 ± 0.9) against the catalytic pockets of proteinaceous allergens. These compounds portray theoretically as agonist molecules when interacts with TLR2 and TLR4 both. All the in silico assessments revealed finally their significant potential as both anti-allergic and anti-inflammatory agents, offering hope for more effective treatments. Moving forward, in vivo testing will be essential to confirm their efficacy and potential for widespread use.