Evidence map›Paper›PMID 24803240›Full record

ArticleChemMedChem2014

Improved bioactivity of antimicrobial peptides by addition of amino-terminal copper and nickel (ATCUN) binding motifs.

M Daben Libardo, Jorge L Cervantes, Juan C Salazar, Alfredo M Angeles-Boza

Open access · greenAbstract read
In one paragraph

Article in ChemMedChem, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
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  4. Review
  5. Article
  6. Activity and Synergy of Cu-ATCUN Antimicrobial Peptides.International journal of molecular sciences · 2022
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Amphiphilic Aminoglycosides as Medicinal Agents.International journal of molecular sciences · 2020
    Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
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  20. 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

4 authors at 3 institutions in 1 country.

M Daben LibardoDepartment of Chemistry, University of Connecticut, Unit 3060, 55 North Eagleville Rd, Storrs, CT 06269 (USA).
Jorge L Cervantes
Juan C Salazar
Alfredo M Angeles-Boza
University of Connecticut · USConnecticut Children's Medical Center · USUConn Health · US

Funding

Phagosomal Signals Shape Inflammatory Responses to B. BurgdorferiR01AI090166 · NIAID · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI SALAZAR, JUAN C · 2011 to 2015
$2.1M
NIAID NIH HHS R01 AI090166
6 · The paper itself

Abstract

Antimicrobial peptides (AMPs) are promising candidates to help circumvent antibiotic resistance, which is an increasing clinical problem. Amino-terminal copper and nickel (ATCUN) binding motifs are known to actively form reactive oxygen species (ROS) upon metal binding. The combination of these two peptidic constructs could lead to a novel class of dual-acting antimicrobial agents. To test this hypothesis, a set of ATCUN binding motifs were screened for their ability to induce ROS formation, and the most potent were then used to modify AMPs with different modes of action. ATCUN binding motif-containing derivatives of anoplin (GLLKRIKTLL-NH2), pro-apoptotic peptide (PAP; KLAKLAKKLAKLAK-NH2), and sh-buforin (RAGLQFPVGRVHRLLRK-NH2) were synthesized and found to be more active than the parent AMPs against a panel of clinically relevant bacteria. The lower minimum inhibitory concentration (MIC) values for the ATCUN-anoplin peptides are attributed to the higher pore-forming activity along with their ability to cause ROS-induced membrane damage. The addition of the ATCUN motifs to PAP also increases its ability to disrupt membranes. DNA damage is the major contributor to the activity of the ATCUN-sh-buforin peptides. Our findings indicate that the addition of ATCUN motifs to AMPs is a simple strategy that leads to AMPs with higher antibacterial activity and possibly to more potent, usable antibacterial agents.

Indexed as

Antimicrobial Cationic PeptidesAmino Acid MotifsAnti-Infective AgentsCopperGram-Negative BacteriaGram-Positive BacteriaNickelPeptide LibraryProtein BindingProtein Structure, SecondaryReactive Oxygen SpeciesAnti-Infective AgentsAntimicrobial Cationic PeptidesCopperNickelPeptide LibraryReactive Oxygen Speciesamino-terminal copper & nickel (ATCUN) binding motifsantimicrobial peptidesbioinorganic chemistrycytotoxicity

Identifiers

PMID24803240
PMCPMC4440792
OpenAlexW1993896935

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.