Structural highlights
Publication Abstract from PubMedAntimicrobial activity is being increasingly linked to amyloid fibril formation, suggesting physiological roles for some human amyloids, which have historically been viewed as strictly pathological agents. This work reports on formation of functional cross-alpha amyloid fibrils of the amphibian antimicrobial peptide uperin 3.5 at atomic resolution, an architecture initially discovered in the bacterial PSMalpha3 cytotoxin. The fibrils of uperin 3.5 and PSMalpha3 comprised antiparallel and parallel helical sheets, respectively, recapitulating properties of beta-sheets. Uperin 3.5 demonstrated chameleon properties of a secondary structure switch, forming mostly cross-beta fibrils in the absence of lipids. Uperin 3.5 helical fibril formation was largely induced by, and formed on, bacterial cells or membrane mimetics, and led to membrane damage and cell death. These findings suggest a regulation mechanism, which includes storage of inactive peptides as well as environmentally induced activation of uperin 3.5, via chameleon cross-alpha/beta amyloid fibrils. The amphibian antimicrobial peptide uperin 3.5 is a cross-alpha/cross-beta chameleon functional amyloid.,Salinas N, Tayeb-Fligelman E, Sammito MD, Bloch D, Jelinek R, Noy D, Uson I, Landau M Proc Natl Acad Sci U S A. 2021 Jan 19;118(3). pii: 2014442118. doi:, 10.1073/pnas.2014442118. PMID:33431675[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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