article · ChemistrySelect
This research evaluates how phenolic compounds isolated from Hibiscus syriacus inhibit the enzyme beta-glucuronidase, combining laboratory assays with computational modelling. Laboratory testing demonstrated that chlorogenic acid and dactylifric acid are potent inhibitors of the enzyme, recording low IC50 values. Kinetic analyses revealed that chlorogenic acid acts via competitive inhibition, whereas dactylifric acid operates through a mixed inhibition mechanism similar to the positive control reference compound. Molecular docking confirmed that both phenolics display strong binding affinities, form extensive polar contacts, and occupy the same binding pocket as the reference drug. Furthermore, 30-nanosecond molecular dynamics simulations showed that both compounds maintain stable trajectories and achieve significant energy stabilisation when bound to the enzyme. Together, these laboratory and computational results identify chlorogenic acid and dactylifric acid as promising beta-glucuronidase inhibitors.
Understanding how natural plant compounds block beta-glucuronidase is a vital step in discovering new medical treatments. By detailing the exact molecular interactions of compounds from Hibiscus syriacus, this work provides clear scientific evidence supporting their ability to target this specific enzyme effectively.
The findings could support early-stage drug discovery programmes seeking natural therapeutic leads to inhibit beta-glucuronidase. Potential users include pharmaceutical developers and natural product researchers. Based on the in vitro assays and molecular dynamics simulations reported, this work represents early-stage laboratory research that remains distant from clinical application.
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Abstract Exploring the intricate mechanisms of β ‐glucuronidase inhibition is essential to advancing the development of novel therapeutic agents. This study extensively evaluated the inhibitory potential of phenolics from Hibiscus syriacus against β ‐glucuronidase using a combination of in vitro and computational approaches. in vitro assays demonstrated that chlorogenic acid and dactylifric acid exhibited significant inhibitory activity, with low IC 50 values of 1.32 ± 0.08 and 10.02 ± 1.38 µM, respectively. Enzyme kinetics analyses revealed that dactylifric acid and the positive control, EGCG, followed a mixed inhibition mechanism, while chlorogenic acid displayed competitive inhibition, as indicated by the intersecting lines in the Lineweaver–Burk plots. Docking studies supported these in vitro findings, with chlorogenic acid and dactylifric acid showing the lowest binding affinities, extensive polar interactions, and occupancy of identical binding sites as the reference drug. A 30 ns molecular dynamics simulation was performed to explore the interaction dynamics between isolated phenolic compounds and β ‐glucuronidase. Evaluation of multiple MD parameters revealed that chlorogenic acid and dactylifric acid exhibited stable trajectories and substantial energy stabilization in their binding with β ‐glucuronidase. These computational findings are consistent with experimental data, supporting chlorogenic acid and dactylifric acid as potential inhibitors of β ‐glucuronidase.
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DOI: 10.1002/slct.202402984
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