Evidence map›Paper›PMID 15904663›Full record

ArticleBiochimica et biophysica acta2005

Antimicrobial activity and membrane selective interactions of a synthetic lipopeptide MSI-843.

Sathiah Thennarasu, Dong-Kuk Lee, Anmin Tan, U Prasad Kari, Ayyalusamy Ramamoorthy

Abstract read
In one paragraph

Article in Biochimica et biophysica acta, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Impact of membrane curvature on amyloid aggregation.Biochimica et biophysica acta. Biomembranes · 2018
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The potential of antimicrobial peptides as biocides.International journal of molecular sciences · 2011
    Review
  17. Article
  18. A miniature mimic of host defense peptides with systemic antibacterial efficacy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010
    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.

Sathiah ThennarasuBiophysics Research Division and Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA.
Dong-Kuk Lee
Anmin Tan
U Prasad Kari
Ayyalusamy Ramamoorthy

Funding

Structure and function of antimicrobial peptidesR01AI054515 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2004 to 2008
$1.3M
NIAID NIH HHS AI054515NIAID NIH HHS R01 AI054515
6 · The paper itself

Abstract

Lipopeptide MSI-843 consisting of the nonstandard amino acid ornithine (Oct-OOLLOOLOOL-NH2) was designed with an objective towards generating non-lytic short antimicrobial peptides, which can have significant pharmaceutical applications. Octanoic acid was coupled to the N-terminus of the peptide to increase the overall hydrophobicity of the peptide. MSI-843 shows activity against bacteria and fungi at micromolar concentrations. It permeabilizes the outer membrane of Gram-negative bacterium and a model membrane mimicking bacterial inner membrane. Circular dichroism investigations demonstrate that the peptide adopts alpha-helical conformation upon binding to lipid membranes. Isothermal titration calorimetry studies suggest that the peptide binding to membranes results in exothermic heat of reaction, which arises from helix formation and membrane insertion of the peptide. 2H NMR of deuterated-POPC multilamellar vesicles shows the peptide-induced disorder in the hydrophobic core of bilayers. 31P NMR data indicate changes in the lipid head group orientation of POPC, POPG and Escherichia colitotal lipid bilayers upon peptide binding. Results from 31P NMR and dye leakage experiments suggest that the peptide selectively interacts with anionic bilayers at low concentrations (up to 5 mol%). Differential scanning calorimetry experiments on DiPOPE bilayers and 31P NMR data from E.coli total lipid multilamellar vesicles indicate that MSI-843 increases the fluid lamellar to inverted hexagonal phase transition temperature of bilayers by inducing positive curvature strain. Combination of all these data suggests the formation of a lipid-peptide complex resulting in a transient pore as a plausible mechanism for the membrane permeabilization and antimicrobial activity of the lipopeptide MSI-843.

Indexed as

Anti-Bacterial AgentsCalorimetryCell MembraneCell Membrane PermeabilityCircular DichroismEscherichia coliKineticsMagnetic Resonance SpectroscopyOrnithinePeptidesProtein Structure, SecondaryTemperatureAnti-Bacterial AgentsOrnithinePeptides

Identifiers

PMID15904663
PMCPMC1550341

What OpenQuestion holds

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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.