Evidence map›Paper›PMID 24837702›Full record

ArticleACS chemical biology2014

Hydrophobicity and helicity regulate the antifungal activity of 14-helical β-peptides.

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

Abstract read
In one paragraph

Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

25 citing papers in PubMed, 61 citations in OpenAlex.

  1. Repositioning Antimicrobial Peptides Against WHO-Priority Fungi.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Peptide foldamer-based inhibitors of the SARS-CoV-2 S protein-human ACE2 interaction.Journal of enzyme inhibition and medicinal chemistry · 2023
    Article
  8. Review
  9. Article
  10. Article
  11. Gut Bacteria of Water Monitor Lizard (Antibiotics (Basel, Switzerland) · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

5 authors at 1 institution in 1 country.

Myung-Ryul LeeDepartment of Chemical and Biological Engineering and ‡Department of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
Namrata Raman
Samuel H Gellman
David M Lynn
Sean P Palecek
University of Wisconsin–Madison · US

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 1R01 AI092225NIAID NIH HHS R01 AI092225
6 · The paper itself

Abstract

Candida albicans is one of the most prevalent fungal pathogens, causing both mucosal candidiasis and invasive candidemia. Antimicrobial peptides (AMPs), part of the human innate immune system, have been shown to exhibit antifungal activity but have not been effective as pharmaceuticals because of low activity and selectivity in physiologically relevant environments. Nevertheless, studies on α-peptide AMPs have revealed key features that can be designed into more stable structures, such as the 14-helix of β-peptide-based oligomers. Here, we report on the ways in which two of those features, hydrophobicity and helicity, govern the activity and selectivity of 14-helical β-peptides against C. albicans and human red blood cells. Our results reveal both antifungal activity and hemolysis to correlate to hydrophobicity, with intermediate levels of hydrophobicity leading to high antifungal activity and high selectivity toward C. albicans. Helical structure-forming propensity further influenced this window of selective antifungal activity, with more stable helical structures eliciting specificity for C. albicans over a broader range of hydrophobicity. Our findings also reveal cooperativity between hydrophobicity and helicity in regulating antifungal activity and specificity. The results of this study provide critical insight into the ways in which hydrophobicity and helicity govern the activity and specificity of AMPs and identify criteria that may be useful for the design of potent and selective antifungal agents.

Indexed as

Antifungal AgentsAntimicrobial Cationic PeptidesCandida albicansCandidiasisDrug DesignHumansHydrophobic and Hydrophilic InteractionsModels, MolecularProtein Structure, SecondaryAntifungal AgentsAntimicrobial Cationic Peptides

Identifiers

PMID24837702
PMCPMC4105187
OpenAlexW2323677389

What OpenQuestion holds

Textmetadata
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.