ArticleLangmuir : the ACS journal of surfaces and colloids2016
The Effect of Lipopolysaccharide Core Oligosaccharide Size on the Electrostatic Binding of Antimicrobial Proteins to Models of the Gram Negative Bacterial Outer Membrane.
Article in Langmuir : the ACS journal of surfaces and colloids, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 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
48 citing papers in PubMed, 94 citations in OpenAlex.
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- When Disinfection Fails: Biocide Tolerance as a Driver ofAntibiotics (Basel, Switzerland) · 2026Review
- Avoiding Mitochondrial Apoptosis by the Bcl-2-Driven Bax Oligomerization on Membrane Surfaces.ACS chemical biology · 2026Article
- Biophysical Modeling of Lipopolysaccharides in Gram-Negative Bacteria: From Atomic to Colloidal Models.International journal of molecular sciences · 2026Review
- Antimicrobial Peptide Activity in Lipid Bilayers with Smooth-Type Lipopolysaccharides.Analytical chemistry · 2026Article
- Breaking the outer membrane barrier: structure, targets, and antimicrobial strategies for Gram-negative bacteria.Frontiers in microbiology · 2026Review
- Humidity-Induced Structural Transformation in Self-Organized Polymer-Surfactant Multilayer Nanofilms.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Multisite binding of bacteriophages on lipopolysaccharides inMicrobiology spectrum · 2025Article
- Combined Forces Against Bacteria: Phages and Antibiotics.Health science reports · 2025Article
- Expanded Gram-Negative Activity of Marinopyrrole A.Pathogens (Basel, Switzerland) · 2025Article
- Depth-Resolved Temperature-Dependent Penetration of Polymyxin B in Phospholipids/Lipopolysaccharide Asymmetric Bilayers.ACS omega · 2025Article
- Article
- Molecular Mechanisms of Bacterial Resistance to Antimicrobial Peptides in the Modern Era: An Updated Review.Microorganisms · 2024Review
- Probing the allosteric NBD-TMD crosstalk in the ABC transporter MsbA by solid-state NMR.Communications biology · 2024Article
- High prevalence of lipopolysaccharide mutants and R2-Pyocin susceptible variants inbioRxiv : the preprint server for biology · 2023Article
- Breaking membrane barriers to neutralize E. coli and K. pneumoniae virulence with PEGylated branched polyethylenimine.Biochimica et biophysica acta. Biomembranes · 2023Article
- Creation of distinctive Bax-lipid complexes at mitochondrial membrane surfaces drives pore formation to initiate apoptosis.Science advances · 2023Article
- Effective Endotoxin Removal from Chitosan That Preserves Chemical Structure and Improves Compatibility with Immune Cells.Polymers · 2023Article
Corrections and comments
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Authors and funding
6 authors at 5 institutions in 2 countries.
Funding
Abstract
Understanding the electrostatic interactions between bacterial membranes and exogenous proteins is crucial to designing effective antimicrobial agents against Gram-negative bacteria. Here we study, using neutron reflecometry under multiple isotopic contrast conditions, the role of the uncharged sugar groups in the outer core region of lipopolysaccharide (LPS) in protecting the phosphate-rich inner core region from electrostatic interactions with antimicrobial proteins. Models of the asymmetric Gram negative outer membrane on silicon were prepared with phopshatidylcholine (PC) in the inner leaflet (closest to the silicon), whereas rough LPS was used to form the outer leaflet (facing the bulk solution). We show how salt concentration can be used to reversibly alter the binding affinity of a protein antibiotic colicin N (ColN) to the anionic LPS confirming that the interaction is electrostatic in nature. By examining the interaction of ColN with two rough LPS types with different-sized core oligosaccharide regions we demonstrate the role of uncharged sugars in blocking short-range electrostatic interactions between the cationic antibiotics and the vulnerable anionic phosphate groups.
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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.