Evidence map›Paper›PMID 19672319›Full record

ArticleSoft matter2008

Protegrin interaction with lipid monolayers: Grazing incidence X-ray diffraction and X-ray reflectivity study.

Frances Neville, Yuji Ishitsuka, Chris S Hodges, Oleg Konovalov, Alan J Waring, Robert Lehrer, Ka Yee C Lee, David Gidalevitz

Open access · greenAbstract read
In one paragraph

Article in Soft matter, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.5field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Cyclization Improves Membrane Permeation by Antimicrobial Peptoids.Langmuir : the ACS journal of surfaces and colloids · 2016
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. 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
  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

8 authors at 5 institutions in 3 countries.

Frances NevilleAddress, School of Process, Environmental and Materials Engineering, University of Leeds, Leeds, LS2 9JT, UK.
Yuji Ishitsuka
Chris S Hodges
Oleg Konovalov
Alan J Waring
Robert Lehrer
Ka Yee C Lee
David Gidalevitz
Chicago Institute for Psychoanalysis · USEuropean Synchrotron Radiation Facility · FRUniversity of Leeds · GBIllinois Institute of Technology · USUniversity of California, Los Angeles · US

Funding

Antimicrobial Peptides and their Synthetic Mimics - Investigating the Mechanism oR01AI073892 · NIAID · ILLINOIS INSTITUTE OF TECHNOLOGY · PI GIDALEVITZ, DAVID · 2008 to 2011
$1.2M
NIAID NIH HHS R01 AI073892
6 · The paper itself

Abstract

Interactions of the antimicrobial peptide protegrin-1 (PG-1) with phospholipid monolayers have been investigated by using grazing incidence X-ray diffraction (GIXD) and specular X-ray reflectivity (XR). The structure of a PG-1 film at the air-aqueous interface was also investigated by XR for the first time. Lipid A, dipalmitoyl-phosphatidylglycerol (DPPG) and dipalmitoyl-phosphatidylcholine (DPPC) monolayers were formed at the air-aqueous interface to mimic the surface of the bacterial cell wall and the outer leaflet of the erythrocyte cell membrane, respectively. Experiments were carried out under constant area conditions where the pressure changes upon insertion of peptide into the monolayer. GIXD data suggest that the greatest monolayer disruption produced by PG-1 is seen with the DPPG system at 20 mN/m since the Bragg peaks completely disappear after introduction of PG-1 to the system. PG-1 shows greater insertion into the lipid A system compared to the DPPC system when both films are held at the same initial surface pressure of 20 mN/m. The degree of insertion lessens at 30 mN/m with both DPPC and DPPG monolayer systems. XR data further reveal that PG-1 inserts primarily in the head group region of lipid monolayers. However, only the XR data of the anionic lipids suggest the existence of an additional adsorbed peptide layer below the head group of the monolayer. Overall the data show that the extent of peptide/lipid interaction and lipid monolayer disruption depends not only on the lipid composition of the monolayer, but the packing density of the lipids in the monolayer prior to the introduction of peptide to the subphase.

Identifiers

PMID19672319
PMCPMC2723866
OpenAlexW2128086136

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.