Peptide News Digest

#Biosynthesis

2 stories

Research · View digest

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.

Research · View digest

Nature Communications: Manchester Team Reports Alternative Enzymatic Pathway to Penicillins via Standalone Ligase Plus Engineered IPNS

Saha, Xu, Panda, and Micklefield at the University of Manchester and Manchester Institute of Biotechnology published a Nature Communications paper April 30 describing a fundamentally simpler biosynthetic route to penicillin antibiotics. Instead of the traditional ACV tripeptide assembled by complex non-ribosomal peptide synthetase (NRPS) machinery, the team uses standalone glutathione-style ligase and epimerase enzymes to generate the peptide precursor, then transforms it with an engineered isopenicillin N synthase (IPNS) to produce penicillin G, penicillin V, and ampicillin directly. The pathway sidesteps the semisynthesis steps currently required for these penicillins and could simplify production at scale — material in an AMR landscape where supply economics matter as much as new chemistry.