Kanamycin-Mediated Conformational Dynamics of Outer Membrane Protein TolC.

TolC is a member of the outer membrane efflux proteins (OEPs) family and acts as an exit duct to export proteins, antibiotics, and substrate molecules across the cell membrane. Export of these molecules is evidenced to be brought about through the reversible interactions and binding of substrate-specific drug molecules or antibiotics with TolC and by being open for transport, which afterward leads to cross-resistance. Hence, the binding of kanamycin with TolC was monitored through molecular docking (MD), the structural fluctuations and conformational changes to the atomic level.

Oxidative stress generated at nickel oxide nanoparticle interface results in bacterial membrane damage leading to cell death.

Metal oxide nanoparticles (NPs) have shown enhanced antibacterial effects against many bacteria. Thus, understanding the potential antibacterial effects of nickel oxide nanoparticles (NiO NPs) against Gram-positive and Gram-negative pathogenic bacteria is an urgent need to enable the exploration of NiO NP use in biomedical sciences. To this end, NiO NPs were synthesized by microwave assisted hydrothermal synthesis method.