Evidence map›Paper›PMID 24878450›Full record

ArticleBiochimica et biophysica acta2014

Guanidino groups greatly enhance the action of antimicrobial peptidomimetics against bacterial cytoplasmic membranes.

Konstantin Andreev, Christopher Bianchi, Jonas S Laursen, Linda Citterio, Line Hein-Kristensen, Lone Gram, Ivan Kuzmenko, Christian A Olsen, David Gidalevitz

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2014. 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
4.4field-weighted citation impact, top 6% 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, 79 citations in OpenAlex.

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  16. Structural Changes in Films of Pulmonary Surfactant Induced by Surfactant Vesicles.Langmuir : the ACS journal of surfaces and colloids · 2020
    Article
  17. The Best Peptidomimetic Strategies to Undercover Antibacterial Peptides.International journal of molecular sciences · 2020
    Review
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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

9 authors at 3 institutions in 2 countries.

Konstantin Andreev *Center for Molecular Study of Condensed Soft Matter (μCoSM), Pritzker Institute of Biomedical Science and Engineering and Department of Physics, Illinois Institute of Technology, 3440 S. Dearborn St., Chicago, IL 60616 (USA).
Christopher Bianchi *Center for Molecular Study of Condensed Soft Matter (μCoSM), Pritzker Institute of Biomedical Science and Engineering and Department of Physics, Illinois Institute of Technology, 3440 S. Dearborn St., Chicago, IL 60616 (USA).
Jonas S LaursenDepartment of Chemistry, Technical University of Denmark, Kemitorvet 207, DK-2800 Kgs. Lyngby (Denmark).
Linda CitterioDepartment of Systems Biology, Technical University of Denmark, Matematiktorvet 301, DK-2800 Kgs. Lyngby (Denmark).
Line Hein-Kristensen, National Food Institute, Technical University of Denmark, Søltofts Plads 221, DK-2800, Kgs Lyngby (Denmark).
Lone GramDepartment of Systems Biology, Technical University of Denmark, Matematiktorvet 301, DK-2800 Kgs. Lyngby (Denmark).
Ivan KuzmenkoAdvanced Photon Source, Argonne National Laboratory, 9700 S. Cass Ave., Lemont, IL 60439 (USA).
Christian A OlsenDepartment of Chemistry, Technical University of Denmark, Kemitorvet 207, DK-2800 Kgs. Lyngby (Denmark).
David GidalevitzCenter for Molecular Study of Condensed Soft Matter (μCoSM), Pritzker Institute of Biomedical Science and Engineering and Department of Physics, Illinois Institute of Technology, 3440 S. Dearborn St., Chicago, IL 60616 (USA).
Technical University of Denmark · DKIllinois Institute of Technology · USArgonne National Laboratory · 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

Antimicrobial peptides or their synthetic mimics are a promising class of potential new antibiotics. Herein we assess the effect of the type of cationic side chain (i.e., guanidino vs. amino groups) on the membrane perturbing mechanism of antimicrobial α-peptide-β-peptoid chimeras. Langmuir monolayers composed of 1,2-dipalmitoyl-sn-glycero-3-phosphatidylglycerol (DPPG) were used to model cytoplasmic membranes of both Gram-positive and Gram-negative bacteria, while lipopolysaccharide Kdo2-lipid A monolayers were mimicking the outer membrane of Gram-negative species. We report the results of the measurements using an array of techniques, including high-resolution synchrotron surface X-ray scattering, epifluorescence microscopy, and in vitro antimicrobial activity to study the molecular mechanisms of peptidomimetic interaction with bacterial membranes. We found guanidino group-containing chimeras to exhibit greater disruptive activity on DPPG monolayers than the amino group-containing analogues. However, this effect was not observed for lipopolysaccharide monolayers where the difference was negligible. Furthermore, the addition of the nitrobenzoxadiazole fluorophore did not reduce the insertion activity of these antimicrobials into both model membrane systems examined, which may be useful for future cellular localization studies.

Indexed as

Anti-Infective AgentsBacteriaCell MembraneGuanidineLipopolysaccharidesPeptidomimeticsPhosphatidylglycerols1,2-dipalmitoylphosphatidylglycerolAnti-Infective AgentsGuanidineKdo2-lipid ALipopolysaccharidesPeptidomimeticsPhosphatidylglycerolsAntimicrobial peptidomimeticsBacterial membraneGuanidinium cationPeptide–peptoid chimerasPhosphatidylglycerolX-ray scattering

Identifiers

PMID24878450
PMCPMC4125507
OpenAlexW2014573030

What OpenQuestion holds

Textmetadata
LicenceTDM
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.