Evidence map›Paper›PMID 16997872›Full record

ArticleBiophysical journal2006

Antimicrobial peptides temporins B and L induce formation of tubular lipid protrusions from supported phospholipid bilayers.

Yegor A Domanov, Paavo K J Kinnunen

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

35 citing papers in PubMed, 105 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Stability of multilamellar lipid tubules in excess water.European biophysics journal : EBJ · 2023
    Article
  5. Temporins: Multifunctional Peptides from Frog Skin.International journal of molecular sciences · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Synergistic Action of Antimicrobial Lung Proteins againstInternational journal of molecular sciences · 2021
    Article
  10. Article
  11. Review
  12. The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  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

2 authors at 1 institution in 1 country.

Yegor A DomanovHelsinki Biophysics & Biomembrane Group, Medical Biochemistry/Institute of Biomedicine, University of Helsinki, Helsinki, Finland.
Paavo K J Kinnunen
University of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The binding of the antimicrobial peptides temporins B and L to supported lipid bilayer (SLB) model membranes composed of phosphatidylcholine and phosphatidylglycerol (4:1, mol/mol) caused the formation of fibrillar protrusions, visible by fluorescent microscopy of both a fluorescent lipid analog and a labeled peptide. Multicolor imaging at low peptide-to-lipid ratios (P/L < approximately 1:5) revealed an initial in-plane segregation of membrane-bound peptide and partial exclusion of lipid from the peptide-enriched areas. Subsequently, at higher P/L numerous flexible lipid fibrils were seen growing from the areas enriched in lipid. The fibrils have diameters <250 nm and lengths of up to approximately 1 mm. Fibril formation reduces the in-plane heterogeneity and results in a relatively even redistribution of bound peptide over the planar bilayer and the fibrils. Physical properties of the lipid fibrils suggest that they have a tubular structure. Our data demonstrate that the peptide-lipid interactions alone can provide a driving force for the spontaneous membrane shape transformations leading to tubule outgrowth and elongation. Further experiments revealed the importance of positive curvature strain in the tubulation process as well as the sufficient positive charge on the peptide (>/=+2). The observed membrane transformations could provide a simplified in vitro model for morphogenesis of intracellular tubular structures and intercellular connections.

Indexed as

Anti-Infective AgentsAntimicrobial Cationic PeptidesLipid BilayersPeptidesPhosphatidylcholinesPhosphatidylglycerolsPorosityProteinsAnti-Infective AgentsAntimicrobial Cationic PeptidesLipid BilayersPeptidesPhosphatidylcholinesPhosphatidylglycerolsProteinstemporintemporin L, Rana temporaria

Identifiers

PMID16997872
PMCPMC1779916
OpenAlexW2005312734

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.