Abstract Description

Neisseria gonorrhoeae relies on the β-barrel assembly machinery (BAM) for the folding and insertion of the outer membrane proteins (OMPs), further imperative for its survival and virulence. Among the BAM subunits, BamE plays a stabilizing role, interacting with BamA and BamD to complete the Bam functional complex. Disrupting BamE significantly impairs OMP insertion, consequently reducing virulence and improving antibiotic susceptibility. . Protein-protein docking of the native BamE chains (chain A and B) was performed to characterize this interaction interface. Subsequently, 4,5-dicaffeoylquinic acid, apigenin-7-glucoside, carvacrol and quercetin were docked, followed by molecular dynamics simulations to evaluate their stability and binding dynamics. Post-dynamic analysis revealed strong interactions between the test phytochemicals and the BamE chainB, resulting in conformational vicissitudes that led to reduced protein-protein docking scores after interaction with 4,5-dicaffeoylquinic acid, apigenin-7-glucoside, and carvacrol. This highlights the potential of these compounds to destabilize BamE chain interactions, providing a promising strategy for disrupting the BAM complex and reducing insertion of OMPs liable for virulence.