Insect Peptide Thanatin Jams the NDM-1 Superbug Enzyme Without Stripping Its Zinc, NMR Study Shows
Using NMR spectroscopy, docking, and simulations, researchers reported in Communications Chemistry that the antimicrobial peptide thanatin binds beside the catalytic groove of NDM-1, an enzyme that lets bacteria destroy carbapenem antibiotics, and inhibits it by restricting a flexible loop while both zinc ions stay bound. In bacterial assays the effect partly restored carbapenem sensitivity, cutting viable cell output by 50% even with high enzyme levels. The work is lab-only.