ArticleProceedings of the National Academy of Sciences of the United States of America2017
Lipid topology and electrostatic interactions underpin lytic activity of linear cationic antimicrobial peptides in membranes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 85 citations in OpenAlex.
- A unified framework for potency-oriented AMP discovery via multi-modal learning and guided sequence synthesis.PLoS computational biology · 2026Article
- C-Terminal Nucleobase Modification Amplifies Peptide-Mediated Liposome Fusion.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Article
- Membrane Pore Formation by Peptides Studied by Fluorescence Techniques.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Lipidated peptides and the limits of chemical control.Frontiers in chemistry · 2026Article
- A "Detachable Polyanionic Protective Shell" Enveloping Photodynamic Cationic Nanoassemblies for Keratitis Treatment.Research (Washington, D.C.) · 2026Article
- Tutorial: guidelines for the use of machine learning methods to mine genomes and proteomes for antibiotic discovery.Nature protocols · 2025Review
- The Role of Flexibility in the Bioactivity of Short α-Helical Antimicrobial Peptides.Antibiotics (Basel, Switzerland) · 2025Review
- 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
- Article
- Antiviral activity of the host defense peptide piscidin 1: investigating a membrane-mediated mode of action.Frontiers in chemistry · 2024Article
- Peptide Flexibility and the Hydrophobic Moment are Determinants to Evaluate the Clinical Potential of Magainins.The Journal of membrane biology · 2023Article
- Electrochemiluminescence Imaging of Liposome Permeabilization by an Antimicrobial Peptide: Melittin.Chemical & biomedical imaging · 2023Article
- The Unusual Aggregation and Fusion Activity of the Antimicrobial Peptide W-BP100 in Anionic Vesicles.Membranes · 2023Article
- Heterogeneous Structural Disturbance of Cell Membrane by Peptides with Modulated Hydrophobic Properties.Pharmaceutics · 2022Article
- Matching amino acids membrane preference profile to improve activity of antimicrobial peptides.Communications biology · 2022Article
- An N-capping asparagine-lysine-proline (NKP) motif contributes to a hybrid flexible/stable multifunctional peptide scaffold.Chemical science · 2022Article
- Measuring Thousands of Single-Vesicle Leakage Events Reveals the Mode of Action of Antimicrobial Peptides.Analytical chemistry · 2022Article
- Simulations reveal that antimicrobial BP100 induces local membrane thinning, slows lipid dynamics and favors water penetration.RSC advances · 2022Article
- Thermodynamic Modeling of Solvent-Assisted Lipid Bilayer Formation Process.Micromachines · 2022Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Linear cationic antimicrobial peptides are a diverse class of molecules that interact with a wide range of cell membranes. Many of these peptides disrupt cell integrity by forming membrane-spanning pores that ultimately lead to their death. Despite these peptides high potency and ability to evade acquired bacterial drug resistance, there is a lack of knowledge on their selectivity and activity mechanisms. Such an understanding would provide an informative framework for rational design and could lead to potential antimicrobial therapeutic targets. In this paper, we use a high-throughput microfluidic platform as a quantitative screen to assess peptide activity and selectivity by precisely controlling exposure to vesicles with lipid compositions that mimic both bacterial and mammalian cell membranes. We explore the complexity of the lipid-peptide interactions governing membrane-disruptive behaviors and establish a link between peptide pore formation and both lipid-peptide charge and topological interactions. We propose a topological model for linear antimicrobial peptide activity based on the increase in membrane strain caused by the continuous adsorption of peptides to the target vesicle coupled with the effects of both lipid-peptide charge and topographical interactions. We also show the validity of the proposed model by investigating the activity of two prototypical linear cationic peptides: magainin 2 amide (which is selective for bacterial cells) and melittin (which targets both mammalian and bacterial cells indiscriminately). Finally, we propose the existence of a negative feedback mechanism that governs the pore formation process and controls the membrane's apparent permeability.
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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.