Evidence map›Paper›PMID 29638118›Full record

ArticleBiochemistry2018

Activity of Antimicrobial Peptide Aggregates Decreases with Increased Cell Membrane Embedding Free Energy Cost.

Rongfeng Zou, Xiaomin Zhu, Yaoquan Tu, Junchen Wu, Markita P Landry

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 35 citations in OpenAlex.

  1. Antibacterial Activities of Predicted AMP inInternational journal of molecular sciences · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Current pharmaceutical biotechnology · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Heliyon · 2023
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Aggregation State of Synergistic Antimicrobial Peptides.The journal of physical chemistry letters · 2020
    Article
  19. Review
  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

5 authors at 3 institutions in 3 countries.

Rongfeng ZouKey Laboratory for Advanced Materials & Institute of Fine Chemicals, School of Chemistry and Molecular Engineering , East China University of Science and Technology , Shanghai 200237 , China.ORCID 0000-0003-1988-7898
Xiaomin ZhuKey Laboratory for Advanced Materials & Institute of Fine Chemicals, School of Chemistry and Molecular Engineering , East China University of Science and Technology , Shanghai 200237 , China.
Yaoquan TuDivision of Theoretical Chemistry and Biology, School of Biotechnology , KTH Royal Institute of Technology , SE-10691 Stockholm , Sweden.
Junchen WuKey Laboratory for Advanced Materials & Institute of Fine Chemicals, School of Chemistry and Molecular Engineering , East China University of Science and Technology , Shanghai 200237 , China.
Markita P LandryDepartment of Chemical and Bio-molecular Engineering , University of California Berkeley , 476 Stanley Hall , Berkeley , United States.ORCID 0000-0002-5832-8522
East China University of Science and Technology · CNKTH Royal Institute of Technology · SEQB3 · US

Funding

Single-Molecule Imaging of Biological Trauma:Cytokine-Based Intracellular CommunicationR35GM128922 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI LANDRY, MARKITA · 2019 to 2023
$2.0M
NIGMS NIH HHS R35 GM128922
6 · The paper itself

Abstract

Antimicrobial peptides (AMPs) are a promising alternative to antibiotics for mitigating bacterial infections, in light of increasing bacterial resistance to antibiotics. However, predicting, understanding, and controlling the antibacterial activity of AMPs remain a significant challenge. While peptide intramolecular interactions are known to modulate AMP antimicrobial activity, peptide intermolecular interactions remain elusive in their impact on peptide bioactivity. Herein, we test the relationship between AMP intermolecular interactions and antibacterial efficacy by controlling AMP intermolecular hydrophobic and hydrogen bonding interactions. Molecular dynamics simulations and Gibbs free energy calculations in concert with experimental assays show that increasing intermolecular interactions via interpeptide aggregation increases the energy cost for the peptide to embed into the bacterial cell membrane, which in turn decreases the AMP antibacterial activity. Our findings provide a route for predicting and controlling the antibacterial activity of AMPs against Gram-negative bacteria via reductions of intermolecular AMP interactions.

Indexed as

Antimicrobial Cationic PeptidesCell MembraneEnergy MetabolismGram-Negative BacteriaHumansMolecular Dynamics SimulationProtein AggregatesAntimicrobial Cationic PeptidesProtein Aggregates

Identifiers

PMID29638118
PMCPMC10493161
OpenAlexW2796650346

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.