Abstract
AbstractObjectiveAeromonas hydrophila, a leading pathogen of aquatic organisms, poses a significant challenge in terms of effective and safe inhibition.MethodsThrough 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.ResultFurther 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.ConclusionConsequently, our discovery sheds new light on exploring the molecular mechanism through which emodin displays antimicrobial activity against A. hydrophila.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
