ArticleEuropean biophysics journal : EBJ2008
Investigations into the ability of the peptide, HAL18, to interact with bacterial membranes.
Article in European biophysics journal : EBJ, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed.
- Marine Invertebrate Antimicrobial Peptides and Their Potential as Novel Peptide Antibiotics.Marine drugs · 2023Review
- Evaluation of the Efficiency of Random and Diblock Methacrylate-Based Amphiphilic Cationic Polymers against Major Bacterial Pathogens Associated with Cystic Fibrosis.Antibiotics (Basel, Switzerland) · 2023Article
- In silico identification of two peptides with antibacterial activity against multidrug-resistant Staphylococcus aureus.NPJ biofilms and microbiomes · 2022Article
- Article
- The rumen microbiome: an underexplored resource for novel antimicrobial discovery.NPJ biofilms and microbiomes · 2017Article
- Membrane interaction of antimicrobial peptides using E. coli lipid extract as model bacterial cell membranes and SFG spectroscopy.Chemistry and physics of lipids · 2015Article
- Biomechanics and thermodynamics of nanoparticle interactions with plasma and endosomal membrane lipids in cellular uptake and endosomal escape.Langmuir : the ACS journal of surfaces and colloids · 2014Article
- Effect of salt on the interaction of Hal18 with lipid membranes.European biophysics journal : EBJ · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Halocidin was isolated from hemocytes, Halocynthia aurantium as a heterodimeric peptide consisting of two alpha-helical subunits, Hal15 and Hal18. Hal18 was shown to have antibacterial properties against Bacillus subtilis (MLC = 15 microM) and Escherichia coli (MLC = 100 microM). The peptide was shown to produce stable monolayers, which were characteristic of alpha-helical peptides predicted to orientate parallel to the surface of the interface. Constant area assays showed that Hal18 was surface active (4 microM) inducing surface pressure changes >30 mN m(-1) characteristic of membrane interactive peptides. The peptide induced stable surface pressure changes in monolayers that were mimetic of B. subtilis membranes (circa 7 mN m(-1)) and E. coli membrane-mimics (circa 4 mN m(-1)). Hal18 inserted readily into zwitterionic DOPE and anionic DOPG monolayers inducing surface pressure changes circa 8 mN m(-1) in both cases, providing evidence that interaction is not headgroup specific. Thermodynamic analysis of compression isotherms showed that the presence of Hal18 destabilised B. subtilis membranes (DeltaG (Mix) > 0), which is in contrast to its stabilising effect on E. coli lipid extract implying the differential antimicrobial efficacy may be driven by lipid packing.
Indexed as
Identifiers
18600320What OpenQuestion holds
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.