Evidence map›Paper›PMID 28695731›Full record

ArticleACS infectious diseases2017

Investigating the Interaction of Octapeptin A3 with Model Bacterial Membranes.

Mei-Ling Han, Hsin-Hui Shen, Karl A Hansford, Elena K Schneider, Sivashangarie Sivanesan, Kade D Roberts, Philip E Thompson, Anton P Le Brun, Yan Zhu, Marc-Antoine Sani and 7 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS infectious diseases, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

12 citing papers in PubMed, 33 citations in OpenAlex.

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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

17 authors at 6 institutions in 2 countries.

Mei-Ling HanDrug Development and Innovation, Drug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University , Parkville 3052, Victoria Australia.ORCID 0000-0002-0861-2437
Hsin-Hui Shen
Karl A HansfordInstitute for Molecular Bioscience, The University of Queensland , Brisbane, Queensland 4072, Australia.
Elena K SchneiderDrug Development and Innovation, Drug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University , Parkville 3052, Victoria Australia.ORCID 0000-0001-6044-4824
Sivashangarie SivanesanDrug Development and Innovation, Drug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University , Parkville 3052, Victoria Australia.
Kade D RobertsDrug Development and Innovation, Drug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University , Parkville 3052, Victoria Australia.
Philip E ThompsonDrug Development and Innovation, Drug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University , Parkville 3052, Victoria Australia.
Anton P Le BrunBragg Institute, Australian Nuclear Science and Technology Organisation, Locked Bag 2001, Kirrawee DC, New South Wales 2232, Australia.
Yan ZhuDrug Development and Innovation, Drug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University , Parkville 3052, Victoria Australia.
Marc-Antoine SaniSchool of Chemistry, Bio21 Institute, University of Melbourne , Melbourne, Victoria 3010, Australia.
Frances SeparovicSchool of Chemistry, Bio21 Institute, University of Melbourne , Melbourne, Victoria 3010, Australia.ORCID 0000-0002-6484-2763
Mark A T BlaskovichInstitute for Molecular Bioscience, The University of Queensland , Brisbane, Queensland 4072, Australia.ORCID 0000-0001-9447-2292
Mark A BakerPriority Research Centre in Reproductive Science, School of Environmental and Life Sciences, University of Newcastle , Callaghan, New South Wales 2308, Australia.
Samuel M MoskowitzVertex Pharmaceuticals, 50 Northern Avenue, Boston, Massachusetts 02210, United States.
Matthew A CooperInstitute for Molecular Bioscience, The University of Queensland , Brisbane, Queensland 4072, Australia.ORCID 0000-0003-3147-3460
Jian Li
Tony VelkovDrug Development and Innovation, Drug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University , Parkville 3052, Victoria Australia.ORCID 0000-0002-0017-7952
Monash University · AUThe University of Queensland · AUThe University of Melbourne · AUAustralian Nuclear Science and Technology Organisation · AUUniversity of Newcastle Australia · AUVertex Pharmaceuticals (United States) · US

Funding

Targeting superbugs: discovery and development of new broad-spectrum lipopeptidesR01AI098771 · NIAID · MONASH UNIVERSITY · PI LI, JIAN · 2012 to 2016
$4.3M
Targeting MDR hetero-resistant Gram-negatives: PK/PD for rational combinationsR01AI079330 · NIAID · MONASH UNIVERSITY · PI NATION, ROGER L. · 2008 to 2011
$2.2M
Discovery of Polymyxin-based Antibacterial Agents Active Against Multi-Drug ResisR33AI098731 · NIAID · UNIVERSITY OF QUEENSLAND · PI COOPER, MATTHEW A, LASH, LAWRENCE H. · 2014 to 2016
$945k
NIAID NIH HHS R01 AI079330NIAID NIH HHS R01 AI098771NIAID NIH HHS R33 AI098731
6 · The paper itself

Abstract

Octapeptins are cyclic lipopeptides with a broader spectrum of activity against fungi and polymyxin-resistant Gram-negative and Gram-positive bacteria. In the present study, we investigated the interaction of octapeptin A3 with asymmetric outer membrane models of Gram-negative pathogen Pseudomonas aeruginosa using neutron reflectometry, together with fluorimetric and calorimetry methods. For the first time, our neutron reflectometry results reveal that the interaction of octapeptin A3 with the Gram-negative outer membrane involves an initial transient polar interaction with the phospholipid and lipid A headgroups, followed by the penetration of the entire octapeptin molecule into the fatty acyl core of the outer membrane. This mechanism contrasts with that of polymyxin B, which specifically targets lipid A, whereas octapeptins appear to target both lipid A and phospholipids. Furthermore, the mechanism of octapeptins does not appear to be highly dependent on an initial complementary electrostatic interaction with lipid A, which accounts for their ability to bind to lipid A of polymyxin-resistant Gram-negative bacteria that is modified with cationic moieties that act to electrostatically repel the cationic polymyxin molecule. The presented findings shed new light on the mechanism whereby octapeptins penetrate the outer membrane of polymyxin-resistant Gram-negative pathogens and highlight their potential as candidates for development as new antibiotics against problematic multi-drug-resistant pathogens.

Indexed as

1,2-DipalmitoylphosphatidylcholineCarbohydrate ConformationCell MembraneDrug Resistance, Multiple, BacterialLipid ALipid BilayersLipopeptidesPolymyxin BProtein BindingPseudomonas aeruginosaUnilamellar Liposomes1,2-Dipalmitoylphosphatidylcholinecolfosceril palmitateLipid ALipid BilayersLipopeptidesoctapeptin antibioticsPolymyxin BUnilamellar Liposomesmode of actionmultidrug resistanceoctapeptinpolymyxin

Identifiers

PMID28695731
PMCPMC5955700
OpenAlexW2735152854

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.