ArticleeLife2020
Effect of helical kink in antimicrobial peptides on membrane pore formation.
Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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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
39 citing papers in PubMed.
- Recent progress in the structure-activity relationship of antibacterial peptoids.RSC advances · 2026Review
- Computational design of antimicrobial peptide nanopores.Nature chemical biology · 2026Article
- A Localization-Based Motif Combination Approach To the Design of Antimicrobial Peptides Targeting Gram-Positive and Gram-Negative Bacteria.Probiotics and antimicrobial proteins · 2026Article
- Mechanistic Insights into Human Defensin Antimicrobial Activity from Membrane Simulations.The Journal of membrane biology · 2026Article
- From Membrane Composition to Antimicrobial Strategies: Experimental and Computational Approaches to AMP Design and Selectivity.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
- Identification and Characterization of an In Silico Designed Membrane-Active Peptide with Antiviral Properties.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Overcoming multidrug resistance: antimicrobial peptides as a next-generation therapeutic strategy.Frontiers in cellular and infection microbiology · 2026Review
- Antimicrobial peptides in the era of resistance: integrating AI-driven design, host-microbe interactions, and nanotechnological delivery.Frontiers in microbiology · 2026Review
- Membrane Pore Formation by Peptides Studied by Fluorescence Techniques.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Structure of a barrel-stave pore formed by magainin-2 reveals anion selectivity and zipper-mediated assembly.Scientific reports · 2025Article
- Amino Acid Substitutions in Bacteriocin Lactolisterin BU Reveal Functional Domains Involved in Biological Activity AgainstMolecules (Basel, Switzerland) · 2025Article
- Effect of Tau Fragment and Membrane Interactions on Membrane Permeabilization and Peptide Aggregation.Membranes · 2025Article
- Protease production by Serratia liquefaciens NRC1 using fish gut waste as a sustainable approach to antimicrobial peptide generation and combating Candida auris acquired resistance.Microbial cell factories · 2025Article
- Discovery of Novel Genes Encoding Antimicrobial Peptides from theInternational journal of molecular sciences · 2025Article
- The Role of Flexibility in the Bioactivity of Short α-Helical Antimicrobial Peptides.Antibiotics (Basel, Switzerland) · 2025Review
- Article
- Antimicrobial Peptide with a Bent Helix Motif Identified in Parasitic FlatwormInternational journal of molecular sciences · 2024Article
- Helicity-directed recognition of bacterial phospholipid via radially amphiphilic antimicrobial peptides.Science advances · 2024Article
- A Critical Review of Short Antimicrobial Peptides from Scorpion Venoms, Their Physicochemical Attributes, and Potential for the Development of New Drugs.The Journal of membrane biology · 2024Review
- Strategic Single-Residue Substitution in the Antimicrobial Peptide Esc(1-21) Confers Activity againstACS infectious diseases · 2024Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Every cell is protected by a semipermeable membrane. Peptides with the right properties, for example Antimicrobial peptides (AMPs), can disrupt this protective barrier by formation of leaky pores. Unfortunately, matching peptide properties with their ability to selectively form pores in bacterial membranes remains elusive. In particular, the proline/glycine kink in helical peptides was reported to both increase and decrease antimicrobial activity. We used computer simulations and fluorescence experiments to show that a kink in helices affects the formation of membrane pores by stabilizing toroidal pores but disrupting barrel-stave pores. The position of the proline/glycine kink in the sequence further controls the specific structure of toroidal pore. Moreover, we demonstrate that two helical peptides can form a kink-like connection with similar behavior as one long helical peptide with a kink. The provided molecular-level insight can be utilized for design and modification of pore-forming antibacterial peptides or toxins.
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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.