t α‐mangostin rapidly
disrupted the integrity of the cytoplasmic membrane leading to loss of intracellular components in a
concentration-dependent manner. Molecular dynamic simulations revealed that isoprenyl groups were important
to reduce the free energy for the burial of the hydrophobic phenyl ring of α-mangostin into the lipid bilayer of
the membrane resulting in membrane breakdown and increased permeability. Thus, we suggest that direct interactions
of α-mangostin with the bacterial membrane are responsible for the rapid concentration-dependent membrane
disruption and bactericidal action.