Evidence map›Paper›PMID 26287212›Full record

ArticlePharmaceuticals (Basel, Switzerland)2015

Antifungal Activity of 14-Helical β-Peptides against Planktonic Cells and Biofilms of Candida Species.

Namrata Raman, Myung-Ryul Lee, David M Lynn, Sean P Palecek

Abstract read
In one paragraph

Article in Pharmaceuticals (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Frontiers in microbiology · 2022
    Article
  6. Article
  7. Pathogenesis and Clinical Relevance ofFrontiers in microbiology · 2020
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Translocation of cell-penetrating peptides into Candida fungal pathogens.Protein science : a publication of the Protein Society · 2017
    Article
  14. Review
  15. Candida glabrata Biofilms: How Far Have We Come?Journal of fungi (Basel, Switzerland) · 2017
    Review
  16. Article
  17. Article
  18. 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.

Namrata RamanDepartment of Chemical and Biological Engineering, University of Wisconsin-Madison, 1415 Engineering Drive, Madison, WI 53706, USA. nraman2@wisc.edu.
Myung-Ryul LeeDepartment of Chemical and Biological Engineering, University of Wisconsin-Madison, 1415 Engineering Drive, Madison, WI 53706, USA. nraman2@wisc.edu.
David M LynnDepartment of Chemical and Biological Engineering, University of Wisconsin-Madison, 1415 Engineering Drive, Madison, WI 53706, USA. dlynn@engr.wisc.edu.
Sean P PalecekDepartment of Chemical and Biological Engineering, University of Wisconsin-Madison, 1415 Engineering Drive, Madison, WI 53706, USA. palecek@engr.wisc.edu.

Funding

Prevention of C. Albicans Biofilms by Beta-Peptide Release From Thin FilmsR01AI092225 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI PALECEK, SEAN P · 2011 to 2015
$1.8M
NIAID NIH HHS R01 AI092225
6 · The paper itself

Abstract

Candida albicans is the most prevalent cause of fungal infections and treatment is further complicated by the formation of drug resistant biofilms, often on the surfaces of implanted medical devices. In recent years, the incidence of fungal infections by other pathogenic Candida species such as C. glabrata, C. parapsilosis and C. tropicalis has increased. Amphiphilic, helical β-peptide structural mimetics of natural antimicrobial α-peptides have been shown to exhibit specific planktonic antifungal and anti-biofilm formation activity against C. albicans in vitro. Here, we demonstrate that β-peptides are also active against clinically isolated and drug resistant strains of C. albicans and against other opportunistic Candida spp. Different Candida species were susceptible to β-peptides to varying degrees, with C. tropicalis being the most and C. glabrata being the least susceptible. β-peptide hydrophobicity directly correlated with antifungal activity against all the Candida clinical strains and species tested. While β-peptides were largely ineffective at disrupting existing Candida biofilms, hydrophobic β-peptides were able to prevent the formation of C. albicans, C. glabrata, C. parapsilosis and C. tropicalis biofilms. The broad-spectrum antifungal activity of β-peptides against planktonic cells and in preventing biofilm formation suggests the promise of this class of molecules as therapeutics.

Indexed as

antifungalantimicrobial peptidebiofilmsCandida albicansCandida glabrataCandida parapsilosisCandida tropicalishydrophobicityβ-peptide

Identifiers

PMID26287212
PMCPMC4588179

What OpenQuestion holds

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LicenceCC BY
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.