Evidence map›Paper›PMID 39563817›Full record

ArticleACS medicinal chemistry letters2024

Hybrids of Membrane-Translocating Antimicrobial Peptides Show Enhanced Activity through Membrane Permeabilization.

Giulia F Trevellin, JuYoung Kwag, Michelle L Shui, Hannah Klim, Valentina Alvarez, Louise E O Darling, Donald E Elmore

Abstract read
In one paragraph

Article in ACS medicinal chemistry letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. 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

7 authors.

Giulia F TrevellinBiochemistry Program, Wellesley College, 106 Central St., Wellesley, Massachusetts 02481, United States.
JuYoung KwagDepartment of Chemistry, Wellesley College, 106 Central St., Wellesley, Massachusetts 02481, United States.
Michelle L ShuiDepartment of Chemistry, Wellesley College, 106 Central St., Wellesley, Massachusetts 02481, United States.
Hannah KlimBiochemistry Program, Wellesley College, 106 Central St., Wellesley, Massachusetts 02481, United States.
Valentina AlvarezBiochemistry Program, Wellesley College, 106 Central St., Wellesley, Massachusetts 02481, United States.
Louise E O DarlingBiochemistry Program, Wellesley College, 106 Central St., Wellesley, Massachusetts 02481, United States.ORCID https://orcid.org/0000-0002-7798-8024
Donald E ElmoreBiochemistry Program, Wellesley College, 106 Central St., Wellesley, Massachusetts 02481, United States.ORCID https://orcid.org/0000-0002-8723-8710

Funding

Systematic Design of Histone-Derived Antimicrobial PeptidesR15AI169210 · NIAID · WELLESLEY COLLEGE · PI ELMORE, DONALD E. · 2022 to 2022
$455k
NIAID NIH HHS R15 AI169210
6 · The paper itself

Abstract

Antimicrobial peptides (AMPs) hold promise as useful tools to combat bacterial infection. Hybrid peptides, made by linking two independent AMPs together through peptide bonds, have the potential for enhancing antimicrobial activity. Here we explore hybrids created by combining two histone-derived antimicrobial peptides (HDAPs), BF2 and DesHDAP1, that each translocate across bacterial membranes. Our work represents the first systematic approach considering the activity and mechanism of hybrids made from two translocating AMPs. BF2/DesHDAP1 hybrids showed increased antimicrobial activity against both Gram-positive and Gram-negative bacteria compared with the parent peptides and no cytotoxicity against eukaryotic cells. Introducing amino acid linkers between the parent peptides did not further enhance the antibacterial activity. The increased antimicrobial activity comes from a mechanistic shift, as hybrid peptides show decreased translocation across bacterial cell membranes but increased membrane permeabilization compared to BF2 and DesHDAP1. These observations lay the groundwork for the further design of hybrid AMPs made from translocating peptides.

Identifiers

PMID39563817
PMCPMC11571015

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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.