ArticleProceedings of the National Academy of Sciences of the United States of America2013
Common mechanism unites membrane poration by amyloid and antimicrobial peptides.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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Who cites it
77 citing papers in PubMed, 181 citations in OpenAlex.
- The Many Lives of a Single Sequence: Functional Plasticity Through Amyloid Polymorphism.Sub-cellular biochemistry · 2026Review
- Antimicrobial Peptides as Cross-Seeding Modulators at the Neurodegenerative-Infectious Interface.Research (Washington, D.C.) · 2026Review
- Human amylin is a potent antimicrobial peptide that exhibits antimicrobial synergism with the amyloid beta protein.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025Article
- Antimicrobial peptides in post-harvest management of fruits.Journal of food science and technology · 2025Review
- Efficacy ofCurrent research in food science · 2025Article
- Lipid vesicle-based molecular robots.Lab on a chip · 2024Review
- Molecular guidelines for promising antimicrobial agents.Scientific reports · 2024Article
- Lipid oxidation controls peptide self-assembly near membranes through a surface attraction mechanism.Chemical science · 2023Article
- Propranolol induces large-scale remodeling of lipid bilayers: tubules, patches, and holes.RSC advances · 2023Article
- Testing Antimicrobial Properties of Selected Short Amyloids.International journal of molecular sciences · 2023Article
- Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases.Computational and structural biotechnology journal · 2023Review
- Amyloid peptides with antimicrobial and/or microbial agglutination activity.Applied microbiology and biotechnology · 2022Review
- Zn(II) binding to pramlintide results in a structural kink, fibril formation and antifungal activity.Scientific reports · 2022Article
- Human islet amyloid polypeptide: A therapeutic target for the management of type 2 diabetes mellitus.Journal of pharmaceutical analysis · 2022Review
- Repurposing of intestinal defensins as multi-target, dual-function amyloid inhibitorsChemical science · 2022Article
- pH- and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils.Nature communications · 2022Article
- Intracellular mechanism of antimicrobial peptide HJH-3 againstRSC advances · 2022Article
- Cross-seeding between Aβ and SEVI indicates a pathogenic link and gender difference between alzheimer diseases and AIDS.Communications biology · 2022Article
- Evolving and assembling to pierce through: Evolutionary and structural aspects of antimicrobial peptides.Computational and structural biotechnology journal · 2022Review
- Dynorphin A induces membrane permeabilization by formation of proteolipidic pores. Insights from electrophysiology and computational simulations.Computational and structural biotechnology journal · 2022Article
17 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Poration of bacterial membranes by antimicrobial peptides such as magainin 2 is a significant activity performed by innate immune systems. Pore formation by soluble forms of amyloid proteins such as islet amyloid polypeptide (IAPP) is implicated in cell death in amyloidoses. Similarities in structure and poration activity of these two systems suggest a commonality of mechanism. Here, we investigate and compare the mechanisms by which these peptides induce membrane leakage and bacterial cell death through the measurement of liposome leakage kinetics and bacterial growth inhibition. For both systems, leakage occurs through the nucleation-dependent formation of stable membrane pores. Remarkably, we observe IAPP and magainin 2 to be fully cross-cooperative in the induction of leakage and inhibition of bacterial growth. The effects are dramatic, with mixtures of these peptides showing activities >100-fold greater than simple sums of the activities of individual peptides. Direct protein-protein interactions cannot be the origin of cooperativity, as IAPP and its enantiomer D-IAPP are equally cross-cooperative. We conclude that IAPP and magainin 2 induce membrane leakage and cytotoxicity through a shared, cross-cooperative, tension-induced poration mechanism.
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Registered trials
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.