Molecular mechanism of emodin in inhibiting the activity of Aeromonas hydrophila via AtpE

Abstract Objective Aeromonas hydrophila , a leading pathogen of aquatic organisms, poses a significant challenge in terms of effective and safe inhibition. Methods Through the method of experiments and molecular simulations, we discovered that emodin effectively inhibits the A. hydrophila via the binding of emodin with AtpE (ATP synthase subunit C). Bacterial inhibition experiments show that emodin effectively inhibits the activity and growth of A. hydrophila . Result Further molecular docking and molecular dynamics simulation revealed that emodin binds directly to AtpE. More specifically, it binds to certain residues of AtpE, including TYR73, LEU70, ALA13, TYR10, MET17, and ALA14, ultimately leading to inhibition of activity. Conclusion Consequently, our discovery sheds new light on exploring the molecular mechanism through which emodin displays antimicrobial activity against A. hydrophila .