ArticleProceedings of the National Academy of Sciences of the United States of America2021
The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 62 citations in OpenAlex.
- Article
- Article
- Enhancing the Antimicrobial Potency of Self-Assembling Antibiotics by Co-Assembly-Based Aggregation Modulation.Macromolecular bioscience · 2026Article
- A functional amyloid scaffold shapes insect egg coats.bioRxiv : the preprint server for biology · 2026Article
- Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026Review
- Antimicrobial Peptides as Cross-Seeding Modulators at the Neurodegenerative-Infectious Interface.Research (Washington, D.C.) · 2026Review
- Structural and Functional Versatility of the Amyloidogenic Non-Amidated Variant of the Antimicrobial Peptide Citropin 1.3.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- From Pathology to Materials Science and Engineering: Harnessing the Amyloid State for Biotechnological Applications.ACS applied materials & interfaces · 2025Review
- Antimicrobial peptides: structure, functions and translational applications.Nature reviews. Microbiology · 2025Review
- Purification tags markedly affect self-aggregation of CPEB3.FEBS letters · 2025Article
- Article
- Amphipathic Antimicrobial Peptides Illuminate a Reciprocal Relationship Between Self-assembly and Cytolytic Activity.Angewandte Chemie (International ed. in English) · 2025Article
- Differential Effects of Lipid Bilayers on αPSM Peptide Functional Amyloid Formation.International journal of molecular sciences · 2023Article
- Staphylococcus aureus functional amyloids catalyze degradation of β-lactam antibiotics.Nature communications · 2023Article
- Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023Review
- Aggregation of Amyloidogenic Peptide Uperin-Molecular Dynamics Simulations.Molecules (Basel, Switzerland) · 2023Article
- Fragment-BasedACS bio & med chem Au · 2023Article
- Lipid oxidation controls peptide self-assembly near membranes through a surface attraction mechanism.Chemical science · 2023Article
- Article
- Bacterial Lectin FimH and Its Aggregation Hot-Spots: An Alternative Strategy against UropathogenicPharmaceutics · 2023Article
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Authors and funding
8 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antimicrobial 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-α amyloid fibrils of the amphibian antimicrobial peptide uperin 3.5 at atomic resolution, an architecture initially discovered in the bacterial PSMα3 cytotoxin. The fibrils of uperin 3.5 and PSMα3 comprised antiparallel and parallel helical sheets, respectively, recapitulating properties of β-sheets. Uperin 3.5 demonstrated chameleon properties of a secondary structure switch, forming mostly cross-β 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-α/β amyloid fibrils.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.