Evidence map›Paper›PMID 19278255›Full record

ArticleJournal of medicinal chemistry2009

Effect of ring size on conformation and biological activity of cyclic cationic antimicrobial peptides.

Masoud Jelokhani-Niaraki, Leslie H Kondejewski, Laura C Wheaton, Robert S Hodges

Open access · greenAbstract read
In one paragraph

Article in Journal of medicinal chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

14 citing papers in PubMed, 47 citations in OpenAlex.

  1. Probing theRSC chemical biology · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Peptide oligomers from ultra-short peptides using sortase.Biochemistry and biophysics reports · 2017
    Article
  8. Synthesis, spectral and extended spectrum beta-lactamase studies of transition metal tetraaza macrocyclic complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017
    Article
  9. Article
  10. Article
  11. Interactions of disulfide-constrained cyclic tetrapeptides with Cu(2+).Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013
    Article
  12. Article
  13. Article
  14. 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 2 countries.

Masoud Jelokhani-NiarakiDepartment of Chemistry, Wilfrid Laurier University, Waterloo, Ontario, Canada.
Leslie H Kondejewski
Laura C Wheaton
Robert S Hodges
University of Saskatchewan · CAUniversity of Colorado Denver · USWilfrid Laurier University · CA

Funding

Design of New AntimicrobialsR01AI067296 · NIAID · UNIVERSITY OF COLORADO DENVER · PI HODGES, ROBERT S · 2008 to 2012
$1.8M
NIAID NIH HHS NIHR01-AI-067296NIAID NIH HHS R01 AI067296
6 · The paper itself

Abstract

In a series of cyclic peptides based on GS10, an analogue of gramicidin S (GS), the ring size was varied from 10 to 16 amino acids. Alternative addition of basic and hydrophobic amino acids to the original GS10 construct generated a variety of even-numbered rings, i.e., GS10 [cyclo-(VKLdYPVKLdYP)], GS12 [cyclo-(VKLKdYPKVKLdYP)], GS14 [cyclo-(VKLKVdYPLKVKLdYP), and GS16 [cyclo-(VKLKVKdYPKLKVKLdYP)] (d stands for d-enantiomers). The odd-numbered analogues (11-, 13-, and 15-mers) were derived from these four peptides by either addition or deletion of single basic (Lys) or hydrophobic (Leu or Val) amino acids. The resulting peptides, divided into three groups on the basis of peptide ring size (10- to 12-meric, 13- and 14-meric, and 15- and 16-meric), illustrated a diverse spectrum of biological activity correlated to their ring size, degree of beta-structure disruption, charge, hydrophobicity, amphipathicity, and affinity for lipid membranes. Two of these peptides with potent antimicrobial activities and high therapeutic indexes (4.5- to 10-fold compared with GS) are promising candidates for development of broad-spectrum antibiotics.

Indexed as

Anti-Bacterial AgentsAntifungal AgentsAntimicrobial Cationic PeptidesFungiGramicidinGram-Negative BacteriaGram-Positive BacteriaHemolysisHumansHydrophobic and Hydrophilic InteractionsLeucineLysineMicrobial Sensitivity TestsModels, MolecularMolecular ConformationPeptides, CyclicAnti-Bacterial AgentsAntifungal AgentsAntimicrobial Cationic PeptidesGramicidinLeucineLysinePeptides, CyclicValine

Identifiers

PMID19278255
PMCPMC2759687
OpenAlexW2030068856

What OpenQuestion holds

Textmetadata
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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.