ArticleScientific reports2018
Tuneable poration: host defense peptides as sequence probes for antimicrobial mechanisms.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed.
- Probing theRSC chemical biology · 2026Article
- Functional reconstitution of bacterial ESCRT-III protein PspA identifies key regions in membrane binding and remodeling.Protein science : a publication of the Protein Society · 2025Article
- Leaflet by Leaflet Synergistic Effects of Antimicrobial Peptides on Bacterial and Mammalian Membrane Models.The journal of physical chemistry letters · 2023Article
- Enhanced and Stem-Cell-Compatible Effects of Nature-Inspired Antimicrobial Nanotopography and Antimicrobial Peptides to Combat Implant-Associated Infection.ACS applied nano materials · 2023Article
- Switching Cytolytic Nanopores into Antimicrobial Fractal Ruptures by a Single Side Chain Mutation.ACS nano · 2021Article
- Flowering Poration-A Synergistic Multi-Mode Antibacterial Mechanism by a Bacteriocin Fold.iScience · 2020Article
- Innate Inspiration: Antifungal Peptides and Other Immunotherapeutics From the Host Immune Response.Frontiers in immunology · 2020Review
- Antimicrobial Susceptibility Testing of Antimicrobial Peptides to Better Predict Efficacy.Frontiers in cellular and infection microbiology · 2020Review
- Article
- A microfluidic platform for the characterisation of membrane active antimicrobials.Lab on a chip · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
15 authors.
Funding
Abstract
The spread of antimicrobial resistance stimulates discovery strategies that place emphasis on mechanisms circumventing the drawbacks of traditional antibiotics and on agents that hit multiple targets. Host defense peptides (HDPs) are promising candidates in this regard. Here we demonstrate that a given HDP sequence intrinsically encodes for tuneable mechanisms of membrane disruption. Using an archetypal HDP (cecropin B) we show that subtle structural alterations convert antimicrobial mechanisms from native carpet-like scenarios to poration and non-porating membrane exfoliation. Such distinct mechanisms, studied using low- and high-resolution spectroscopy, nanoscale imaging and molecular dynamics simulations, all maintain strong antimicrobial effects, albeit with diminished activity against pathogens resistant to HDPs. The strategy offers an effective search paradigm for the sequence probing of discrete antimicrobial mechanisms within a single HDP.
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