Evidence map›Paper›PMID 32913118›Full record

ArticleThe Journal of biological chemistry2020

Simulations of octapeptin-outer membrane interactions reveal conformational flexibility is linked to antimicrobial potency.

Xukai Jiang, Kai Yang, Bing Yuan, Bin Gong, Lin Wan, Nitin A Patil, James D Swarbrick, Kade D Roberts, Falk Schreiber, Lushan Wang and 2 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

9 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Polymyxin B1 within theBiophysical reviews · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. 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

12 authors at 6 institutions in 4 countries.

Xukai JiangBiomedicine Discovery Institute, Infection & Immunity Program, Department of Microbiology, Monash University, Melbourne, Victoria, Australia.
Kai YangCenter for Soft Condensed Matter Physics and Interdisciplinary Research & School of Physical Science and Technology, Soochow University, Suzhou, China.
Bing YuanCenter for Soft Condensed Matter Physics and Interdisciplinary Research & School of Physical Science and Technology, Soochow University, Suzhou, China.
Bin GongSchool of Software, Shandong University, Jinan, China.
Lin WanSchool of Software, Shandong University, Jinan, China.
Nitin A PatilBiomedicine Discovery Institute, Infection & Immunity Program, Department of Microbiology, Monash University, Melbourne, Victoria, Australia.
James D SwarbrickDepartment of Pharmacology and Therapeutics, University of Melbourne, Melbourne, Victoria, Australia.
Kade D RobertsBiomedicine Discovery Institute, Infection & Immunity Program, Department of Microbiology, Monash University, Melbourne, Victoria, Australia.
Falk SchreiberDepartment of Computer and Information Science, University of Konstanz, Konstanz, Germany.
Lushan WangState Key Laboratory of Microbial Technology, Shandong University, Qingdao, China.
Tony VelkovDepartment of Pharmacology and Therapeutics, University of Melbourne, Melbourne, Victoria, Australia. Electronic address: tony.velkov@unimelb.edu.au.
Jian LiBiomedicine Discovery Institute, Infection & Immunity Program, Department of Microbiology, Monash University, Melbourne, Victoria, Australia. Electronic address: jian.li@monash.edu.
Australian Regenerative Medicine Institute · AUShandong University · CNSoochow University · CNThe University of Melbourne · AUDiscovery Institute · USUniversity of Konstanz · DE

Funding

Targeting the Urgent Need for New Antibiotics against Gram-negative ‘Superbugs’R01AI132154 · NIAID · MONASH UNIVERSITY · PI LI, JIAN, VELKOV, TONY · 2017 to 2021
$4.3M
NIAID NIH HHS R01 AI132154
6 · The paper itself

Abstract

The octapeptins are lipopeptide antibiotics that are structurally similar to polymyxins yet retain activity against polymyxin-resistant Gram-negative pathogens, suggesting they might be used to treat recalcitrant infections. However, the basis of their unique activity is unclear because of the difficulty in generating high-resolution experimental data of the interaction of antimicrobial peptides with lipid membranes. To elucidate these structure-activity relationships, we employed all-atom molecular dynamics simulations with umbrella sampling to investigate the conformational and energetic landscape of octapeptins interacting with bacterial outer membrane (OM). Specifically, we examined the interaction of octapeptin C4 and FADDI-115, lacking a single hydroxyl group compared with octapeptin C4, with the lipid A-phosphoethanolamine modified OM of

Indexed as

Molecular Dynamics SimulationAcinetobacter baumanniiCell MembraneLipopeptidesStructure-Activity RelationshipLipopeptidesoctapeptin antibioticsantibiotic actionantibiotic resistanceantimicrobial resistanceconformational changeconformational transitiondrug designGram-negative bacteriamolecular dynamicsoctapeptinpolymyxin

Identifiers

PMID32913118
PMCPMC7681018
OpenAlexW3085392726

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.