Abstract
BackgroundAntirrhinum majus (Snapdragon) is a perennial Mediterranean-native plant that is commonly used for mass display. Few reports acknowledged the traditional use of A. majus for its medicinal and therapeutic effects. Herein, we assess the impact of A. majus’s sample preparation and extraction methods on the plant-aerial parts’ phytochemical contents and antimicrobial activity. Furthermore, the microbial targets of the extracts’ secondary metabolites are inspected using molecular docking simulations. MethodsThe leaves and flowers of A. majus were prepared as fresh and air-dried samples, then extracted using cold maceration and hot reflux, respectively. Extracts with the best phytochemical profiles were selected to test their antimicrobial activities against Bacillus subtilis, Staphylococcus aureus, Enterobacter aerogenes, Escherichia coli and Candida albicans. Besides, molecular docking of 66 reported isolated compounds was conducted against various microbial targets. ResultsThe dried-refluxed samples revealed a massive deterioration in their phytochemical profiles, whereas the macerated flowers extract exhibited the highest total phenolic content and antimicrobial activity against all tested bacterial strains. However, both flowers and leaves extracts showed similar minimum inhibitory and lethal concentrations against C. albicans. Molecular docking studies revealed that chlorogenic acid, chalcononaringenin 4’-glucoside, 3,4,2’,4’,6’-pentahydroxy-chalcone 4’-glucoside, apigenin-7-glucuronide, and luteolin-7-glucuronide were the lead compounds in expressing the antimicrobial activity. Yet, A. majus’s compounds could neither inhibit the 30S ribosomal subunit nor muramyl ligase E. ConclusionOur results suggest that cold maceration of A. majus fresh aerial parts gave higher flavonoid and phenolic content contributing to its antimicrobial properties. These flavonoids and phenolic compounds are predicted to have a crucial role in inhibiting fungal sterol 14-demethylase, and bacterial dihydropteroate synthase and gyrase B subunit proteins.
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