Evidence map›Paper›PMID 29621496›Full record

ArticleBiochimica et biophysica acta. Biomembranes2018

Hydrophobic interactions modulate antimicrobial peptoid selectivity towards anionic lipid membranes.

Konstantin Andreev, Michael W Martynowycz, Mia L Huang, Ivan Kuzmenko, Wei Bu, Kent Kirshenbaum, David Gidalevitz

Abstract readComparative Study
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
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

29 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Cellular Uptake of Phase-Separating Peptide Coacervates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Microbiology spectrum · 2021
    Article
  17. Review
  18. Article
  19. Structural Changes in Films of Pulmonary Surfactant Induced by Surfactant Vesicles.Langmuir : the ACS journal of surfaces and colloids · 2020
    Article
  20. The Best Peptidomimetic Strategies to Undercover Antibacterial Peptides.International journal of molecular sciences · 2020
    Review
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.

Konstantin AndreevDepartment of Physics, Center for Molecular Study of Condensed Soft Matter (μCoSM), Pritzker Institute of Biomedical Science and Engineering, Illinois Institute of Technology, 3440 South Dearborn Street, Chicago, IL 60616, United States.
Michael W MartynowyczDepartment of Physics, Center for Molecular Study of Condensed Soft Matter (μCoSM), Pritzker Institute of Biomedical Science and Engineering, Illinois Institute of Technology, 3440 South Dearborn Street, Chicago, IL 60616, United States; Advanced Photon Source, Argonne National Laboratory, 9700 South Cass Avenue, Lemont, IL 60439, United States.
Mia L HuangDepartment of Chemistry, New York University, 100 Washington Square East, New York, NY 10003, United States.
Ivan KuzmenkoAdvanced Photon Source, Argonne National Laboratory, 9700 South Cass Avenue, Lemont, IL 60439, United States.
Wei BuThe Center for Advanced Radiation Sources (CARS), University of Chicago, Chicago, IL 60637, United States.
Kent KirshenbaumDepartment of Chemistry, New York University, 100 Washington Square East, New York, NY 10003, United States.
David GidalevitzDepartment of Physics, Center for Molecular Study of Condensed Soft Matter (μCoSM), Pritzker Institute of Biomedical Science and Engineering, Illinois Institute of Technology, 3440 South Dearborn Street, Chicago, IL 60616, United States. Electronic address: gidalevitz@iit.edu.

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

Hydrophobic interactions govern specificity for natural antimicrobial peptides. No such relationship has been established for synthetic peptoids that mimic antimicrobial peptides. Peptoid macrocycles synthesized with five different aromatic groups are investigated by minimum inhibitory and hemolytic concentration assays, epifluorescence microscopy, atomic force microscopy, and X-ray reflectivity. Peptoid hydrophobicity is determined using high performance liquid chromatography. Disruption of bacterial but not eukaryotic lipid membranes is demonstrated on the solid supported lipid bilayers and Langmuir monolayers. X-ray reflectivity studies demonstrate that intercalation of peptoids with zwitterionic or negatively charged lipid membranes is found to be regulated by hydrophobicity. Critical levels of peptoid selectivity are demonstrated and found to be modulated by their hydrophobic groups. It is suggested that peptoids may follow different optimization schemes as compared to their natural analogues.

Indexed as

AnionsAntimicrobial Cationic PeptidesChromatography, High Pressure LiquidErythrocytesGram-Negative BacteriaGram-Positive BacteriaHemolysisHumansHydrophobic and Hydrophilic InteractionsLipid BilayersMembrane LipidsMethicillin-Resistant Staphylococcus aureusMicrobial Sensitivity TestsMicroscopy, Atomic ForceMolecular StructureStatic ElectricityAnionsAntimicrobial Cationic PeptidesLipid BilayersMembrane LipidsAFMAntimicrobial peptoidsCytotoxicityHydrophobicityLipid membranesX-ray scattering

Identifiers

PMID29621496
PMCPMC5957517

What OpenQuestion holds

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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.