Hoose, A; Garcia-Ruiz, J; Blake, C; Lally, C C M; Briones, A; Hoogenboom, B W; Lorenz, C D; Ryadnov, M G (2025) Multi-modal membrane poration by thanatin. Langmuir, 41 (6). pp. 3757-3767.

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Abstract

Antimicrobial resistance motivates the search for antimicrobial agents with multimodal mechanisms of action. Host defence peptides and bacteriocins hold a particular promise in this regard. Amongst many molecules discovered to date, thanatin appears to represent the properties of the two classes in that it, like bacteriocins, adopts a highly stable fold in solution, and, like host defence peptides, exhibits a broad-spectrum antibiotic activity. The peptide is believed to depolarize bacterial outer membranes and inhibit lipopolysaccharide transport, while restoring bacterial susceptibility to β-lactam antibiotics. However, a direct observation of whether and how thanatin affects membranes is lacking. Here we reason that the peptide should promote bacteriocin-like multimodal poration in phospholipid bilayers. We demonstrate that thanatin induces poration with elements of membrane thinning, fractal ruptures and transmembrane channels – a phenomenon common for bacteriocin folds, but atypical of antimicrobial peptides. The results offer a mechanistic insight into the action of antimicrobial agents emerging from different molecular classes but with similar properties.

Item Type:	Article
Subjects:	Biotechnology > Biopharmaceutical Manufacturing and Characterisation
Divisions:	Chemical & Biological Sciences
Identification number/DOI:	10.1021/acs.langmuir.4c03439
Last Modified:	02 Jul 2025 13:56
URI:	https://eprintspublications.npl.co.uk/id/eprint/10191