Jena Chemists Show Pandoraea Bacteria Trim the Lipid Tail Off a Cyclic Peptide to Switch It From Swarming Aid to Iron Scavenger
Researchers at the Leibniz Institute for Natural Product Research and Infection Biology (Leibniz-HKI) and the University of Jena, with senior author Christian Hertweck, reported in Angewandte Chemie International Edition that Pandoraea bacteria, a group that includes opportunistic pathogens, make lipopeptide siderophores called pandorachelins. An enzyme called PdnM removes the fatty-acid tail from pandorachelin B, triggering a rearrangement that contracts its ring into pandorachelin A, a head-to-tail cyclic peptide. The tailed form works as a surfactant that helps the bacteria swarm, while the trimmed form binds iron more tightly but no longer promotes movement. The paper was published online on July 24, 2026 and described by phys.org on September 25; the authors suggested the findings could inform drug delivery, but no medical use has been tested.