Evidence map›Paper›PMID 32166806›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2020

Synergistic Biophysical Techniques Reveal Structural Mechanisms of Engineered Cationic Antimicrobial Peptides in Lipid Model Membranes.

Frank Heinrich, Aria Salyapongse, Akari Kumagai, Fernando G Dupuy, Karpur Shukla, Anja Penk, Daniel Huster, Robert K Ernst, Anna Pavlova, James C Gumbart and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

16 citing papers in PubMed, 18 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

13 authors at 8 institutions in 4 countries.

Frank HeinrichBiological Physics Group, Department of Physics, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.ORCID http://orcid.org/0000-0002-8579-553X
Aria SalyapongseBiological Physics Group, Department of Physics, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.
Akari KumagaiBiological Physics Group, Department of Physics, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.
Fernando G DupuyBiological Physics Group, Department of Physics, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.ORCID http://orcid.org/0000-0002-6799-8528
Karpur ShuklaBiological Physics Group, Department of Physics, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.
Anja PenkInstitute for Medical Physics and Biophysics, Leipzig University, Leipzig, Germany.
Daniel HusterInstitute for Medical Physics and Biophysics, Leipzig University, Leipzig, Germany.ORCID http://orcid.org/0000-0002-3273-0943
Robert K ErnstDepartment of Microbial Pathogenesis, University of Maryland, Baltimore, MD, 21201, USA.ORCID http://orcid.org/0000-0001-5016-8694
Anna PavlovaSchool of Physics, Georgia Institute of Technology, Atlanta, GA, 30332, USA.ORCID http://orcid.org/0000-0002-6527-944X
James C GumbartSchool of Physics, Georgia Institute of Technology, Atlanta, GA, 30332, USA.ORCID http://orcid.org/0000-0002-1510-7842
Berthony DeslouchesDepartment of Environmental and Occupational Health, University of Pittsburgh, Pittsburgh, PA, 15260, USA.ORCID http://orcid.org/0000-0003-4797-7065
Y Peter DiDepartment of Environmental and Occupational Health, University of Pittsburgh, Pittsburgh, PA, 15260, USA.ORCID http://orcid.org/0000-0003-2028-2087
Stephanie Tristram-NagleBiological Physics Group, Department of Physics, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.ORCID http://orcid.org/0000-0003-2271-7056
Carnegie Mellon University · USGeorgia Institute of Technology · USLeipzig University · DEUniversity of Pittsburgh · USConsejo Nacional de Investigaciones Científicas y Técnicas · ARFlame University · INNational Institute of Standards and Technology · USUniversity of Maryland, Baltimore · US

Funding

Novel antimicrobial agents to overcome antibiotic resistant Pseudomonas and MRSA respiratory infectionR01AI133351 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI DI, YUANPU PETER · 2017 to 2021
$2.6M
Determinants and Mechanisms of Efficacy of Peptide Antibiotics as Novel Sepsis TherapyR01GM125917 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI DESLOUCHES, BERTHONY · 2018 to 2022
$2.1M
Dynamic characterization of outer-membrane-protein biogenesis by the BAM and TAM complexesR01GM123169 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI GUMBART, JAMES C. · 2017 to 2021
$1.4M
Membrane Coupling and Dynamic Reorganization of Gag in Viral BuddingR01GM101647 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI LOESCHE, MATHIAS · 2012 to 2015
$1.2M
Carnegie Mellon SURFConsejo Nacional de Innovación, Ciencia y Tecnología Programma de Becas ExternasDeutsche Forschungsgemeinschaft HU 720/15-1, SFB 803Deutsche Forschungsgemeinschaft HU 720/18-1, SFB 803National Science Foundation ACI-1548562National Science Foundation DMR 1332208National Science Foundation OC1-1053575NIAID NIH HHS R01 AI133351NIGMS NIH HHS R01 GM101647NIGMS NIH HHS R01 GM123169NIGMS NIH HHS R01 GM125917NIH HHS R01AI133351NIH HHS R01GM101647NIH HHS R01GM123169NIH HHS R01GM125917NIST Center for Neutron Research 70NANB17H299NIST DOC IMS Program ''Precision Measurement for Integral Membrane Proteins''U.S. Department of Commerce 70NANB13H009
6 · The paper itself

Abstract

In the quest for new antibiotics, two novel engineered cationic antimicrobial peptides (eCAPs) have been rationally designed. WLBU2 and D8 (all 8 valines are the d-enantiomer) efficiently kill both Gram-negative and -positive bacteria, but WLBU2 is toxic and D8 nontoxic to eukaryotic cells. We explore protein secondary structure, location of peptides in six lipid model membranes, changes in membrane structure and pore evidence. We suggest that protein secondary structure is not a critical determinant of bactericidal activity, but that membrane thinning and dual location of WLBU2 and D8 in the membrane headgroup and hydrocarbon region may be important. While neither peptide thins the Gram-negative lipopolysaccharide outer membrane model, both locate deep into its hydrocarbon region where they are primed for self-promoted uptake into the periplasm. The partially α-helical secondary structure of WLBU2 in a red blood cell (RBC) membrane model containing 50 % cholesterol, could play a role in destabilizing this RBC membrane model causing pore formation that is not observed with the D8 random coil, which correlates with RBC hemolysis caused by WLBU2 but not by D8.

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesCell MembraneHemolysisLipopolysaccharidesMembrane LipidsMicrobial Sensitivity TestsProtein Structure, SecondaryPseudomonas aeruginosaAnti-Bacterial AgentsAntimicrobial Cationic PeptidesLipopolysaccharidesMembrane Lipidsdrug designengineered cationic antimicrobial peptidesmembranesneutron reflectivityprotein-lipid interactions

Identifiers

PMID32166806
PMCPMC8146162
OpenAlexW3012183086

What OpenQuestion holds

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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.