Evidence map›Paper›PMID 36139091›Full record

ArticleBiomolecules2022

Where Electrostatics Matter: Bacterial Surface Neutralization and Membrane Disruption by Antimicrobial Peptides SAAP-148 and OP-145.

Djenana Vejzovic, Paulina Piller, Robert A Cordfunke, Jan W Drijfhout, Tobias Eisenberg, Karl Lohner, Nermina Malanovic

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

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  10. Review
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  13. Article
  14. SAAP-148 Oligomerizes into a Hexamer Forming a Hydrophobic Inner Core.Chembiochem : a European journal of chemical biology · 2025
    Article
  15. Article
  16. Article
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  18. Bactericidal Activity toAntibiotics (Basel, Switzerland) · 2023
    Article
  19. 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

7 authors at 2 institutions in 2 countries.

Djenana VejzovicInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50/III, 8010 Graz, Austria.
Paulina PillerInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50/III, 8010 Graz, Austria.
Robert A CordfunkeDepartment of Immunology, Leiden University Medical Center, 2300 ZA Leiden, The Netherlands.
Jan W DrijfhoutDepartment of Immunology, Leiden University Medical Center, 2300 ZA Leiden, The Netherlands.ORCID 0000-0003-4808-5296
Tobias EisenbergInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50/III, 8010 Graz, Austria.
Karl LohnerInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50/III, 8010 Graz, Austria.
Nermina MalanovicInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50/III, 8010 Graz, Austria.ORCID 0000-0002-2903-9369
University of Graz · ATLeiden University Medical Center · NL

Funding

Austrian Science Fund FWF TAI 602
6 · The paper itself

Abstract

The need for alternative treatment of multi-drug-resistant bacteria led to the increased design of antimicrobial peptides (AMPs). AMPs exhibit a broad antimicrobial spectrum without a distinct preference for a specific species. Thus, their mechanism, disruption of fundamental barrier function by permeabilization of the bacterial cytoplasmic membrane is considered to be rather general and less likely related to antimicrobial resistance. Of all physico-chemical properties of AMPs, their positive charge seems to be crucial for their interaction with negatively charged bacterial membranes. Therefore, we elucidate the role of electrostatic interaction on bacterial surface neutralization and on membrane disruption potential of two potent antimicrobial peptides, namely, OP-145 and SAAP-148. Experiments were performed on

Indexed as

Antimicrobial PeptidesEscherichia coliAnti-Bacterial AgentsCell MembraneGram-Negative BacteriaMicrobial Sensitivity TestsPeptidesStatic ElectricityAnti-Bacterial AgentsAntimicrobial PeptidesPeptidesE. coliE. hiraeelectrostatic interactionlipid–peptide interactionmembrane activity

Identifiers

PMID36139091
PMCPMC9496175
OpenAlexW4295106771

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.