Evidence map›Paper›PMID 18293958›Full record

ArticleThe journal of physical chemistry. B2008

Influence of lipid composition on membrane activity of antimicrobial phenylene ethynylene oligomers.

Abhigyan Som, Gregory N Tew

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Designing mimics of membrane active proteins.Accounts of chemical research · 2013
    Article
  16. Cationic antimicrobial polymers and their assemblies.International journal of molecular sciences · 2013
    Review
  17. Antibacterial drug leads targeting isoprenoid biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  18. Article
  19. Article
  20. Antibacterial mechanism of action of arylamide foldamers.Antimicrobial agents and chemotherapy · 2011
    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

2 authors.

Abhigyan SomDepartment of Polymer Science and Engineering, University of Massachusetts, Amherst, 120 Governors Drive, Amherst, Massachusetts 01003, USA.
Gregory N Tew

Funding

Proteomics to Biomimetic Polymers: Engineering PrincipleR01GM065803 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM F · 2002 to 2002
$635k
NIGMS NIH HHS R01 GM065803NIGMS NIH HHS R01-GM-65803
6 · The paper itself

Abstract

Host defense peptides (HDPs), part of the innate immune system, selectively target the membranes of bacterial cells over that of host cells. As a result, their antimicrobial properties have been under intense study. Their selectivity strongly depends on the chemical and mostly structural properties of the lipids that make up different cell membranes. The ability to synthesize HDP mimics has recently been demonstrated. To better understand how these HDP mimics interact with bilayer membranes, three homologous antimicrobial oligomers (AMOs) 1-3 with an m-phenylene ethynylene backbone and alkyl amine side chains were studied. Among them, AMO 1 is nonactive, AMO 2 is specifically active, and AMO 3 is nonspecifically active against bacteria over human red blood cells, a standard model for mammalian cells. The interactions of these three AMOs with liposomes having different lipid compositions are characterized in detail using a fluorescent dye leakage assay. AMO 2 and AMO 3 caused more leakage than AMO 1 from bacteria membrane mimic liposomes composed of PE/PG lipids. The use of E. coli lipid vesicles gave the same results. Further changes of the lipid compositions revealed that AMO 2 has selectively higher affinity toward PE/PG and E. coli lipids than PC, PC/PG or PC/PS lipids, the major components of mammalian cell membranes. In contrast, AMO 3 is devoid of this lipid selectivity and interacts with all liposomes with equal ease; AMO 1 remains inactive. These observations suggest that lipid type and structure are more important in determining membrane selectivity than lipid headgroup charges for this series of HDP mimics.

Indexed as

AlkynesAnti-Bacterial AgentsAntimicrobial Cationic PeptidesEthersAminesBinding, CompetitiveBlood Bactericidal ActivityCardiolipinsCell MembraneEscherichia coliHumansLipidsLiposomesMembrane PotentialsPhosphatidylglycerolsPhosphatidylserinesAlkynesAminesAnti-Bacterial AgentsAntimicrobial Cationic PeptidesCardiolipinsEthersLipidsLiposomesphenyleneethynylenePhosphatidylglycerolsPhosphatidylserines

Identifiers

PMID18293958
PMCPMC3774278

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.