Evidence map›Paper›PMID 27520722›Full record

ArticleNanomedicine : nanotechnology, biology, and medicine2017

Self-assembled cationic amphiphiles as antimicrobial peptides mimics: Role of hydrophobicity, linkage type, and assembly state.

Yingyue Zhang, Ammar Algburi, Ning Wang, Vladyslav Kholodovych, Drym O Oh, Michael Chikindas, Kathryn E Uhrich

Abstract read
In one paragraph

Article in Nanomedicine : nanotechnology, biology, and medicine, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. 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

7 authors.

Yingyue ZhangDepartment of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ, USA.
Ammar AlgburiDepartment of Microbiology and Biochemistry, Rutgers University, New Brunswick, NJ, USA; Department of Microbiology, Veterinary College, Diyala University, Baqubah, Iraq.
Ning WangDepartment of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ, USA.
Vladyslav KholodovychOffice of Advanced Research Computing (OARC), Rutgers University, Piscataway, NJ, USA; Department of Pharmacology, Robert Wood Johnson Medical School, Rutgers University, Piscataway, NJ, USA; Ernest Mario School of Pharmacy, Rutgers University, Piscataway, NJ, USA.
Drym O OhErnest Mario School of Pharmacy, Rutgers University, Piscataway, NJ, USA.
Michael ChikindasSchool of Environmental and Biological Science, Rutgers University, New Brunswick, NJ, USA; Center for Digestive Health, NJ Institute for Food, Nutrition and Health, New Brunswick, NJ, USA.
Kathryn E UhrichDepartment of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ, USA. Electronic address: keuhrich@rutgers.edu.

Funding

Supercomputing: Rutgers' Catalyst for Discovery at the Frontiers of MedicineS10OD012346 · OD · RBHS-NEW JERSEY MEDICAL SCHOOL · PI MICHELSON, LESLIE PAUL · 2015 to 2015
$1.7M
Synthetic AMPs that Control Biofilms of Gram-variable PathogensR21AI126053 · NIAID · RUTGERS, THE STATE UNIV OF N.J. · PI CHIKINDAS, MICHAEL, UHRICH, KATHRYN ELIZABETH · 2016 to 2017
$421k
NIAID NIH HHS R21 AI126053NIH HHS S10 OD012346
6 · The paper itself

Abstract

Inspired by high promise using naturally occurring antimicrobial peptides (AMPs) to treat infections caused by antimicrobial-resistant bacteria, cationic amphiphiles (CAms) were strategically designed as synthetic mimics to overcome associated limitations, including high manufacture cost and low metabolic stability. CAms with facially amphiphilic conformation were expected to demonstrate membrane-lytic properties and thus reduce tendency of resistance development. By systematically tuning the hydrophobicity, CAms with optimized compositions exhibited potent broad-spectrum antimicrobial activity (with minimum inhibitory concentrations in low μg/mL range) as well as negligible hemolytic activity. Electron microscope images revealed the morphological and ultrastructure changes of bacterial membranes induced by CAm treatment and validated their membrane-disrupting mechanism. Additionally, an all-atom molecular dynamics simulation was employed to understand the CAm-membrane interaction on molecular level. This study shows that these CAms can serve as viable scaffolds for designing next generation of AMP mimics as antimicrobial alternatives to combat drug-resistant pathogens.

Indexed as

Antimicrobial Cationic PeptidesAnti-Infective AgentsHemolysisHydrophobic and Hydrophilic InteractionsMicrobial Sensitivity TestsMolecular StructureAnti-Infective AgentsAntimicrobial Cationic PeptidesAntimicrobial activityAntimicrobial peptidesMembrane disruptionSelf-assemblySynthetic mimics

Identifiers

PMID27520722
PMCPMC6849474

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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.