Evidence map›Paper›PMID 14733612›Full record

ArticleThe Biochemical journal2004

Interactions of histatin 5 and histatin 5-derived peptides with liposome membranes: surface effects, translocation and permeabilization.

Alice L Den Hertog, Harro W Wong Fong Sang, Ruud Kraayenhof, Jan G M Bolscher, Wim Van't Hof, Enno C I Veerman, Arie V Nieuw Amerongen

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In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
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  3. Review
  4. Article
  5. Article
  6. Article
  7. A Synergic Potential of Antimicrobial Peptides againstMolecules (Basel, Switzerland) · 2021
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Activity and characterization of a pH-sensitive antimicrobial peptide.Biochimica et biophysica acta. Biomembranes · 2019
    Article
  13. Article
  14. Article
  15. Article
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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

7 authors at 2 institutions in 1 country.

Alice L Den HertogDepartment of Dental Basic Sciences, Section Oral Biochemistry, Academic Centre for Dentistry Amsterdam (ACTA), Vrije Universiteit, Van der Boechorststraat 7, 1081 BT, Amsterdam, The Netherlands. al.denhertog@vumc.nl
Harro W Wong Fong Sang
Ruud Kraayenhof
Jan G M Bolscher
Wim Van't Hof
Enno C I Veerman
Arie V Nieuw Amerongen
Academic Center for Dentistry Amsterdam · NLVrije Universiteit Amsterdam · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A number of cationic antimicrobial peptides, among which are histatin 5 and the derived peptides dhvar4 and dhvar5, enter their target cells and interact with internal organelles. There still are questions about the mechanisms by which antimicrobial peptides translocate across the membrane. We used a liposome model to study membrane binding, translocation and membrane-perturbing capacities of histatin 5, dhvar4 and dhvar5. Despite the differences in amphipathic characters of these peptides, they bound equally well to liposomes, whereas their membrane activities differed remarkably: dhvar4 translocated at the fastest rate, followed by dhvar5, whereas the histatin 5 translocation rate was much lower. The same pattern was seen for the extent of calcein release: highest with dhvar4, less with dhvar5 and almost none with histatin 5. The translocation and disruptive actions of dhvar5 did not seem to be coupled, because translocation occurred on a much longer timescale than calcein release, which ended within a few minutes. We conclude that peptide translocation can occur through peptide-phospholipid interactions, and that this is a possible mechanism by which antimicrobial peptides enter cells. However, the translocation rate was much lower in this model membrane system than that seen in yeast cells. Thus it is likely that, at least for some peptides, additional features promoting the translocation across biological membranes are involved as well.

Indexed as

Cell Membrane PermeabilityAmino Acid SequenceCell MembraneFluoresceinsHistatinsLiposomesMembrane PotentialsMolecular Sequence DataPeptide FragmentsProtein BindingProtein TransportSalivary Proteins and PeptidesTrypsinFluoresceinsfluorexonHistatinsHTN3 protein, humanLiposomesPeptide FragmentsSalivary Proteins and PeptidesTrypsin

Identifiers

PMID14733612
PMCPMC1224109
OpenAlexW2142504461

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.