Evidence map›Paper›PMID 24905681›Full record

ArticleColloids and surfaces. B, Biointerfaces2014

Binding interactions of bacterial lipopolysaccharide and the cationic amphiphilic peptides polymyxin B and WLBU2.

Matthew P Ryder, Xiangming Wu, Greg R McKelvey, Joseph McGuire, Karl F Schilke

Abstract read
In one paragraph

Article in Colloids and surfaces. B, Biointerfaces, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Polymyxin B1 within theBiophysical reviews · 2021
    Review
  8. Article
  9. Review
  10. Antibiofilm peptides as a promising strategy: comparative research.Applied microbiology and biotechnology · 2021
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Matthew P RyderSchool of Chemical, Biological and Environmental Engineering, Oregon State University, Corvallis, OR 97331, United States.
Xiangming WuSchool of Chemical, Biological and Environmental Engineering, Oregon State University, Corvallis, OR 97331, United States.
Greg R McKelveySchool of Chemical, Biological and Environmental Engineering, Oregon State University, Corvallis, OR 97331, United States.
Joseph McGuireSchool of Chemical, Biological and Environmental Engineering, Oregon State University, Corvallis, OR 97331, United States.
Karl F SchilkeSchool of Chemical, Biological and Environmental Engineering, Oregon State University, Corvallis, OR 97331, United States. Electronic address: karl.schilke@oregonstate.edu.

Funding

Microchannel Dialyzer DevelopmentR01EB011567 · NIBIB · OREGON STATE UNIVERSITY · PI JOVANOVIC, GORAN N, MCGUIRE, JOSEPH · 2010 to 2013
$2.3M
NIBIB NIH HHS R01 EB011567NIBIB NIH HHS R01EB011567
6 · The paper itself

Abstract

Passage of blood through a sorbent device for removal of bacteria and endotoxin by specific binding with immobilized, membrane-active, bactericidal peptides holds promise for treating severe blood infections. Peptide insertion in the target membrane and rapid/strong binding is desirable, while membrane disruption and release of degradation products to the circulating blood is not. Here we describe interactions between bacterial endotoxin (lipopolysaccharide, LPS) and the membrane-active, bactericidal peptides WLBU2 and polymyxin B (PmB). Analysis of the interfacial behavior of mixtures of LPS and peptide using air-water interfacial tensiometry and optical waveguide lightmode spectroscopy strongly suggests insertion of intact LPS vesicles by the peptide WLBU2 without vesicle destabilization. In contrast, dynamic light scattering (DLS) studies show that LPS vesicles appear to undergo peptide-induced destabilization in the presence of PmB. Circular dichroism spectra further confirm that WLBU2, which shows disordered structure in aqueous solution and substantially helical structure in membrane-mimetic environments, is stably located within the LPS membrane in peptide-vesicle mixtures. We therefore expect that presentation of WLBU2 at an interface, if tethered in a fashion which preserves its mobility and solvent accessibility, will enable the capture of bacteria and endotoxin without promoting reintroduction of endotoxin to the circulating blood, thus minimizing adverse clinical outcomes. On the other hand, our results suggest no such favorable outcome of LPS interactions with polymyxin B.

Indexed as

AdsorptionAirAmino Acid SequenceAntimicrobial Cationic PeptidesCircular DichroismHydrophobic and Hydrophilic InteractionsKineticsLipopolysaccharidesMolecular Sequence DataMolecular WeightParticle SizePolymyxin BProtein BindingSurface-Active AgentsSurface TensionWaterAntimicrobial Cationic PeptidesLipopolysaccharidesPolymyxin BSurface-Active AgentsWaterWLBU2 peptideCationic amphiphilic peptidesEndotoxinInterfacial tensiometryLipopolysaccharidePolymyxin BSepsisWLBU2

Identifiers

PMID24905681
PMCPMC4113084

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Registered trials

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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.