ArticleBiophysical journal2020
Polymyxin B Loosens Lipopolysaccharide Bilayer but Stiffens Phospholipid Bilayer.
Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
33 citing papers in PubMed, 66 citations in OpenAlex.
- Ib-M1 Antimicrobial Peptide Alters Membrane Permeability and DisruptsMicroorganisms · 2026Article
- Antibiotic Mechanisms and Resistance: Molecular Insights and Therapeutic Strategies.Antibiotics (Basel, Switzerland) · 2026Review
- Polymyxins slow down lateral diffusion of proteins and lipopolysaccharide in the E. coli outer membrane.Communications biology · 2025Article
- Physiologically informed in vitro framework reveals context-dependent combinatory activity of niclosamide-colistin against Gram-negative bacteria.The Journal of antimicrobial chemotherapy · 2025Article
- The Brownian dynamics simulator PyRID for reacting and interacting particles written in Python.Cell reports methods · 2025Article
- Article
- Role of Divalent Ions in Membrane Models of Polymyxin-Sensitive and Resistant Gram-Negative Bacteria.Journal of chemical information and modeling · 2025Article
- Depth-Resolved Temperature-Dependent Penetration of Polymyxin B in Phospholipids/Lipopolysaccharide Asymmetric Bilayers.ACS omega · 2025Article
- Insights into colistin-mediated fluorescence labelling of bacterial LPS.RSC advances · 2024Article
- Characterization of the Antimicrobial Activities ofPharmaceutics · 2023Article
- Synthesis of vancomycin fluorescent probes that retain antimicrobial activity, identify Gram-positive bacteria, and detect Gram-negative outer membrane damage.Communications biology · 2023Article
- Article
- Lipid Microenvironment Modulates the Pore-Forming Ability of Polymyxin B.Antibiotics (Basel, Switzerland) · 2022Article
- Synergistic Membrane Disturbance Improves the Antibacterial Performance of Polymyxin B.Polymers · 2022Article
- Polymyxins induce lipid scrambling and disrupt the homeostasis of Gram-negative bacteria membrane.Biophysical journal · 2022Article
- The ArcAB Two-Component System: Function in Metabolism, Redox Control, and Infection.Microbiology and molecular biology reviews : MMBR · 2022Review
- Distinct lipid membrane interaction and uptake of differentially charged nanoplastics in bacteria.Journal of nanobiotechnology · 2022Article
- Inhibition of MurA Enzyme fromAntibiotics (Basel, Switzerland) · 2021Article
- Polymyxin B1 within theBiophysical reviews · 2021Review
- Structure and Formation Mechanism of Antimicrobial Peptides Temporin B- and L-Induced Tubular Membrane Protrusion.International journal of molecular sciences · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multidrug-resistant Gram-negative bacteria have increased the prevalence of a variety of serious diseases in modern times. Polymyxins are used as the last-line therapeutic options for the treatment of infections. However, the mechanism of action of polymyxins remains in dispute. In this work, we used a coarse-grained molecular dynamics simulation to investigate the mechanism of the cationic antimicrobial peptide polymyxin B (PmB) interacting with both the inner and outer membrane models of bacteria. Our results show that the binding of PmB disturbs the outer membrane by displacing the counterions, decreasing the orientation order of the lipopolysaccharide tail, and creating more lipopolysaccharide packing defects. Upon binding onto the inner membrane, in contrast to the traditional killing mechanism that antimicrobial peptides usually use to induce holes in the membrane, PmBs do not permeabilize the inner membrane but stiffen it by filling up the lipid packing defect, increasing the lipid tail order and the membrane bending rigidity as well as restricting the lipid diffusion. PmBs also mediate intermembrane contact and adhesion. These joint effects suggest that PmBs deprive the biological activity of Gram-negative bacteria by sterilizing the cell.
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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.