Evidence map›Paper›PMID 40073424›Full record

ArticleAngewandte Chemie (International ed. in English)2025

Amphipathic Antimicrobial Peptides Illuminate a Reciprocal Relationship Between Self-assembly and Cytolytic Activity.

Breana Laguera, Martina M Golden, Fengbin Wang, Ordy Gnewou, Abraham Tuachi, Edward H Egelman, William M Wuest, Vincent P Conticello

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026
    Review
  4. Review
  5. Article
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

8 authors.

Breana Laguera *Department of Chemistry, Emory University, Atlanta, GA, 30322, USA.
Martina M Golden *Department of Chemistry, Emory University, Atlanta, GA, 30322, USA.
Fengbin Wang *Biochemistry and Molecular Genetics Department, University of Alabama at Birmingham, Birmingham, AL, 35233, USA.
Ordy GnewouDepartment of Chemistry, Emory University, Atlanta, GA, 30322, USA.
Abraham TuachiDepartment of Chemistry, Emory University, Atlanta, GA, 30322, USA.
Edward H EgelmanDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA, 22908, USA.
William M WuestDepartment of Chemistry, Emory University, Atlanta, GA, 30322, USA.
Vincent P ConticelloDepartment of Chemistry, Emory University, Atlanta, GA, 30322, USA.

Funding

Atlanta Clinical and Translational Science Institute (ACTSI) RenewalUL1TR000454 · NCATS · EMORY UNIVERSITY · PI STEPHENS, DAVID S · 2012 to 2016
$25.8M
Cryo-EM of Helical Protein and Nucleoprotein Polymers at Near Atomic ResolutionR35GM122510 · NIGMS · UNIVERSITY OF VIRGINIA · PI EDWARD H. EGELMAN · 2017 to 2026
$7.3M
Natural Product-Inspired Approaches Toward The Development Of Antivirulence And Species-Specific InhibitorsR35GM119426 · NIGMS · TEMPLE UNIV OF THE COMMONWEALTH · PI William M Wuest · 2016 to 2026
$4.8M
UVA molecular electron microscopy core for the Mid-Atlantic regionU24GM116790 · NIGMS · UNIVERSITY OF VIRGINIA · PI GALKIN, VITOLD, SAMSO, MONTSERRAT · 2017 to 2021
$2.9M
Antimicrobial Resistance and Therapeutic Discovery Training ProgramT32AI106699 · NIAID · EMORY UNIVERSITY · PI Graeme L Conn, Joanna B Goldberg · 2014 to 2026
$2.7M
Molecular Electron Microscopy Core Facility ImprovementsG20RR031199 · NCRR · UNIVERSITY OF VIRGINIA · PI SHUPNIK, MARGARET A · 2010 to 2010
$2.0M
300 keV Liquid Helium Robotic MicroscopeS10RR025067 · NCRR · UNIVERSITY OF VIRGINIA · PI EGELMAN, EDWARD H. · 2009 to 2009
$2.0M
Understanding and using microbial conductive nanowiresR00GM138756 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI WANG, FENGBIN · 2022 to 2024
$895k
Understanding and using microbial conductive nanowiresK99GM138756 · NIGMS · UNIVERSITY OF VIRGINIA · PI WANG, FENGBIN · 2021 to 2022
$130k
National Science Foundation CHE-2108621National Science Foundation DBI-17265NCATS NIH HHS UL1 TR000454NCRR NIH HHS G20 RR031199NCRR NIH HHS S10 RR025067NIAID NIH HHS T32 AI106699NIGMS NIH HHS K99 GM138756NIGMS NIH HHS R00 GM138756NIGMS NIH HHS R35 GM119426NIGMS NIH HHS R35 GM122510NIGMS NIH HHS U24 GM116790NIH HHS AI106699NIH HHS GM119426NIH HHS GM122510NIH HHS GM138756
6 · The paper itself

Abstract

Amphipathic character, encoded within the polar sequence patterns of antimicrobial peptides, is a critical structural feature that influences membrane disruptive behavior. Similarly, polar sequence patterns induce self-assembly of amphipathic peptides, which results in the formation of ordered supramolecular structures. The relationship between self-assembly and membrane activity remains an open question of relevance for the development of effective antimicrobial peptides. Here, we report the structural investigation of a class of lytic peptides that self-assemble into filamentous nanomaterials. CryoEM analysis was employed to determine the structure of one of the filaments, which revealed that the peptides are self-assembled into a bilayer nanotube, in which the interaction between layers of amphipathic α-helices was mediated through hydrophobic interactions. The relative stability of the filament peptide assemblies depended on the influence of sequence modifications on the helical conformation. Antimicrobial assays indicated that cytolytic activity was associated with dynamic disassociation of the filamentous assemblies under the assay conditions. Structural modifications of the peptides that stabilized the filaments abrogated lytic activity. These results illuminate a reciprocal relationship between self-assembly and antimicrobial activity in this class of amphipathic peptides and that reversible assembly was critical for the observation of biological activity.

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesAntimicrobial PeptidesHumansHydrophobic and Hydrophilic InteractionsMicrobial Sensitivity TestsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntimicrobial PeptidesAmphipathic sequenceAntimicrobial peptidecryoEMPolar patternSelf‐assembly

Identifiers

PMID40073424
PMCPMC12088898

What OpenQuestion holds

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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.