Evidence map›Paper›PMID 21641310›Full record

ArticleBiophysical journal2011

Biophysical mechanisms of endotoxin neutralization by cationic amphiphilic peptides.

Yani Kaconis, Ina Kowalski, Jörg Howe, Annemarie Brauser, Walter Richter, Iosu Razquin-Olazarán, Melania Iñigo-Pestaña, Patrick Garidel, Manfred Rössle, Guillermo Martinez de Tejada and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
7.3field-weighted citation impact, top 2% of its field
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

51 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
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  11. Article
  12. Anti-Infective and Anti-Inflammatory Mode of Action of Peptide 19-2.5.International journal of molecular sciences · 2021
    Article
  13. Article
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  15. Article
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  17. The Anti-Microbial Peptide (Lin-SB056-1)Antibiotics (Basel, Switzerland) · 2020
    Article
  18. Review
  19. ACS omega · 2020
    Article
  20. Review
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

12 authors at 5 institutions in 2 countries.

Yani KaconisForschungszentrum Borstel, Leibniz-Zentrum für Medizin und Biowissenschaften, Borstel, Germany.
Ina Kowalski
Jörg Howe
Annemarie Brauser
Walter Richter
Iosu Razquin-Olazarán
Melania Iñigo-Pestaña
Patrick Garidel
Manfred Rössle
Guillermo Martinez de Tejada
Thomas Gutsmann
Klaus Brandenburg
Research Center Borstel - Leibniz Lung Center · DEUniversidad de Navarra · ESEuropean Molecular Biology Laboratory · DEFriedrich Schiller University Jena · DEUniversity of Kaiserslautern · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial endotoxins (lipopolysaccharides (LPS)) are strong elicitors of the human immune system by interacting with serum and membrane proteins such as lipopolysaccharide-binding protein (LBP) and CD14 with high specificity. At LPS concentrations as low as 0.3 ng/ml, such interactions may lead to severe pathophysiological effects, including sepsis and septic shock. One approach to inhibit an uncontrolled inflammatory reaction is the use of appropriate polycationic and amphiphilic antimicrobial peptides, here called synthetic anti-LPS peptides (SALPs). We designed various SALP structures and investigated their ability to inhibit LPS-induced cytokine secretion in vitro, their protective effect in a mouse model of sepsis, and their cytotoxicity in physiological human cells. Using a variety of biophysical techniques, we investigated selected SALPs with considerable differences in their biological responses to characterize and understand the mechanism of LPS inactivation by SALPs. Our investigations show that neutralization of LPS by peptides is associated with a fluidization of the LPS acyl chains, a strong exothermic Coulomb interaction between the two compounds, and a drastic change of the LPS aggregate type from cubic into multilamellar, with an increase in the aggregate sizes, inhibiting the binding of LBP and other mammalian proteins to the endotoxin. At the same time, peptide binding to phospholipids of human origin (e.g., phosphatidylcholine) does not cause essential structural changes, such as changes in membrane fluidity and bilayer structure. The absence of cytotoxicity is explained by the high specificity of the interaction of the peptides with LPS.

Indexed as

Biophysical PhenomenaHydrophobic and Hydrophilic InteractionsAnimalsAntimicrobial Cationic PeptidesBiomimetic MaterialsCell MembraneCytokinesFemaleHorseshoe CrabsHumansLeukocytes, MononuclearLipid BilayersLipopolysaccharidesMicePhospholipidsProtein BindingAntimicrobial Cationic PeptidesCytokinesLipid BilayersLipopolysaccharidesPhospholipids

Identifiers

PMID21641310
PMCPMC3117184
OpenAlexW2008586931

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.