ArticleBiophysical journal2007
Thermodynamic analysis of the lipopolysaccharide-dependent resistance of gram-negative bacteria against polymyxin B.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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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
24 citing papers in PubMed, 60 citations in OpenAlex.
- Lipopolysaccharide and Coagulation Factor XII: Biophysics of Contact Activation in Infection.Seminars in thrombosis and hemostasis · 2026Review
- Broxyquinoline enhances antibacterial activity of colistin and attenuates LPS-induced inflammation.Antimicrobial agents and chemotherapy · 2026Article
- From Membrane Composition to Antimicrobial Strategies: Experimental and Computational Approaches to AMP Design and Selectivity.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
- Differential membrane lipid disruption by lipopeptide antibiotics, colistin and turnercyclamycins.Nature communications · 2026Article
- Interactions between Lipopolysaccharide and Peptide Bacteriocin BacSp222 Influence Their Biological Activities.ACS infectious diseases · 2025Article
- Depth-Resolved Temperature-Dependent Penetration of Polymyxin B in Phospholipids/Lipopolysaccharide Asymmetric Bilayers.ACS omega · 2025Article
- A Comparison between SARS-CoV-2 and Gram-Negative Bacteria-Induced Hyperinflammation and Sepsis.International journal of molecular sciences · 2023Review
- Structure-Activity Relationships of Low Molecular Weight Alginate Oligosaccharide Therapy againstBiomolecules · 2023Article
- Affinity-Guided Isolation and Identification of Procyanidin B2 from Mangosteen (Garcinia mangostana L.) Rinds and its In Vitro LPS Binding and Neutralization Activities.Plant foods for human nutrition (Dordrecht, Netherlands) · 2021Article
- Anti-Infective and Anti-Inflammatory Mode of Action of Peptide 19-2.5.International journal of molecular sciences · 2021Article
- The Beauty of Asymmetric Membranes: Reconstitution of the Outer Membrane of Gram-Negative Bacteria.Frontiers in cell and developmental biology · 2020Article
- Inhibition of Lipopolysaccharide- and Lipoprotein-Induced Inflammation by Antitoxin Peptide Pep19-2.5.Frontiers in immunology · 2018Review
- Inhibitory Effects of Antimicrobial Peptides on Lipopolysaccharide-Induced Inflammation.Mediators of inflammation · 2015Review
- Surface changes and polymyxin interactions with a resistant strain of Klebsiella pneumoniae.Innate immunity · 2014Article
- Resurrecting inactive antimicrobial peptides from the lipopolysaccharide trap.Antimicrobial agents and chemotherapy · 2014Article
- Preclinical investigations reveal the broad-spectrum neutralizing activity of peptide Pep19-2.5 on bacterial pathogenicity factors.Antimicrobial agents and chemotherapy · 2013Article
- Biophysical mechanisms of the neutralization of endotoxins by lipopolyamines.The open biochemistry journal · 2013Article
- Lipopolysaccharide neutralization by antimicrobial peptides: a gambit in the innate host defense strategy.Journal of innate immunity · 2012Review
- Biophysical mechanisms of endotoxin neutralization by cationic amphiphilic peptides.Biophysical journal · 2011Article
- Design, synthesis, and evaluation of a new fluorescent probe for measuring polymyxin-lipopolysaccharide binding interactions.Analytical biochemistry · 2011Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cationic antimicrobial cationic peptides (CAMP) have been found in recent years to play a decisive role in hosts' defense against microbial infection. They have also been investigated as a new therapeutic tool, necessary in particular due to the increasing resistance of microbiological populations to antibiotics. The structural basis of the activity of CAMPs has only partly been elucidated and may comprise quite different mechanism at the site of the bacterial cell membranes or in their cytoplasm. Polymyxin B (PMB) is a CAMP which is effective in particular against Gram-negative bacteria and has been well studied with the aim to understand its interaction with the outer membrane or isolated membrane components such as lipopolysaccharide (LPS) and to define the mechanism by which the peptides kill bacteria or neutralize LPS. Since PMB resistance of bacteria is a long-known phenomenon and is attributed to structural changes in the LPS moiety of the respective bacteria, we have performed a thermodynamic and biophysical analysis to get insights into the mechanisms of various LPS/PMB interactions in comparison to LPS from sensitive strains. In isothermal titration calorimetric (ITC) experiments considerable differences of PMB binding to sensitive and resistant LPS were found. For sensitive LPS the endothermic enthalpy change in the gel phase of the hydrocarbon chains converts into an exothermic reaction in the liquid crystalline phase. In contrast, for resistant LPS the binding enthalpy change remains endothermic in both phases. As infrared data show, these differences can be explained by steric changes in the headgroup region of the respective LPS.
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