Evidence map›Paper›PMID 31067436›Full record

ArticleBiochimica et biophysica acta. Biomembranes2019

Hybrids made from antimicrobial peptides with different mechanisms of action show enhanced membrane permeabilization.

Heidi M Wade, Louise E O Darling, Donald E Elmore

Abstract read
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

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  15. Qualitative and Quantitative Changes toLangmuir : the ACS journal of surfaces and colloids · 2020
    Article
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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

3 authors.

Heidi M WadeDepartment of Chemistry, Wellesley College, Wellesley, MA 02481, United States of America; Biochemistry Program, Wellesley College, Wellesley, MA 02481, United States of America.
Louise E O DarlingBiochemistry Program, Wellesley College, Wellesley, MA 02481, United States of America; Department of Biological Sciences, Wellesley College, Wellesley, MA 02481, United States of America.
Donald E ElmoreDepartment of Chemistry, Wellesley College, Wellesley, MA 02481, United States of America; Biochemistry Program, Wellesley College, Wellesley, MA 02481, United States of America. Electronic address: delmore@wellesley.edu.

Funding

Characterization and Design of Histone-Derived Antimicrobial PeptidesR15AI079685 · NIAID · WELLESLEY COLLEGE · PI ELMORE, DONALD E. · 2010 to 2015
$630k
NIAID NIH HHS R15 AI079685
6 · The paper itself

Abstract

Combining two known antimicrobial peptides (AMPs) into a hybrid peptide is one promising avenue in the design of agents with increased antibacterial activity. However, very few previous studies have considered the effect of creating a hybrid from one AMP that permeabilizes membranes and another AMP that acts intracellularly after translocating across the membrane. Moreover, very few studies have systematically evaluated the order of parent peptides or the presence of linkers in the design of hybrid AMPs. Here, we use a combination of antibacterial measurements, cellular assays and semi-quantitative confocal microscopy to characterize the activity and mechanism for a library of sixteen hybrid peptides. These hybrids consist of permutations of two primarily membrane translocating peptides, buforin II and DesHDAP1, and two primarily membrane permeabilizing peptides, magainin 2 and parasin. For all hybrids, the permeabilizing peptide appeared to dominate the mechanism, with hybrids primarily killing bacteria through membrane permeabilization. We also observed increased hybrid activity when the permeabilizing parent peptide was placed at the N-terminus. Activity data also highlighted the potential value of considering AMP cocktails in addition to hybrid peptides. Together, these observations will guide future design efforts aiming to design more active hybrid AMPs.

Indexed as

Amino Acid SequenceAnti-Bacterial AgentsAnti-Infective AgentsAntimicrobial Cationic PeptidesBacteriaCell MembraneCell Membrane PermeabilityLipid BilayersMagaininsMembrane LipidsMembranesMicrobial Sensitivity TestsMicroscopy, ConfocalPeptidesPhosphatidylcholinesProteinsAnti-Bacterial AgentsAnti-Infective AgentsAntimicrobial Cationic Peptidesbuforin IILipid BilayersMagaininsMembrane Lipidsparasin IPeptidesPhosphatidylcholinesProteinsAntimicrobial peptideHybrid peptideMembrane permeabilizationMembrane translocationPeptide design

Identifiers

PMID31067436
PMCPMC6721965

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Registered trials

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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.