{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T01:03:42Z","timestamp":1790816622095,"version":"4.1.0"},"reference-count":46,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T00:00:00Z","timestamp":1790726400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"},{"start":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T00:00:00Z","timestamp":1790726400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Angew Chem Int Ed"],"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Antimicrobial peptides (AMPs) have long been ascribed the ability to form pores. These structures, some observed, others inferred, vary in their mechanisms of action, though most are associated with lysis. Here, we show that an AMP derived from a truncated staphylococcal \u03b4\u2010toxin can form functional pores that do not cause rapid lysis but, instead, we suggest that they act as self\u2010transport systems. Specifically, a 17\u2010amino acid AMP named STIP3\u20101 was observed to oligomerize and form a unique supramolecular helical assembly with an \u223c14 \u00c5 pore. Substitutions to the STIP3\u20101 peptide abolished our ability to detect pore formation in model membranes and prevented peptide accumulation in\n                    <jats:italic>Staphylococcus aureus<\/jats:italic>\n                    . In the case of G3A and G3Aib variants, the substitutions resulted in stabilization of antiparallel 4\u2010helix bundles rather than a nanotubular assembly characterized by a two\u2010ring structure formed by repeating trimers. MD simulations suggest that Gly may impart versatility in STIP3\u20101 phospholipid binding. Our observation of this remarkable STIP3\u20101 structure expands how we can approach mechanistic and translational studies of AMPs.\n                  <\/jats:p>","DOI":"10.1002\/anie.2822225","type":"journal-article","created":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:27:27Z","timestamp":1790814447000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Supramolecular Assembly of an Antimicrobial Peptide Into a Pore"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4599-5446","authenticated-orcid":false,"given":"Kathyana","family":"Deeyagahage","sequence":"first","affiliation":[{"name":"Department of Veterinary Microbiology University of Saskatchewan  Saskatoon Saskatchewan 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