Evidence map›Paper›PMID 19359494›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

De novo design and in vivo activity of conformationally restrained antimicrobial arylamide foldamers.

Sungwook Choi, Andre Isaacs, Dylan Clements, Dahui Liu, Hyemin Kim, Richard W Scott, Jeffrey D Winkler, William F DeGrado

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing 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

104 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Cyclodextrin derivatives that exhibitRSC medicinal chemistry · 2025
    Article
  5. Fighting Antimicrobial Resistance: Innovative Drugs in Antibacterial Research.Angewandte Chemie (International ed. in English) · 2025
    Review
  6. Review
  7. Turn-Adopting Peptidomimetic as a Formyl Peptide Receptor-1 Antagonist.ACS pharmacology & translational science · 2024
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Staph wars: the antibiotic pipeline strikes back.Microbiology (Reading, England) · 2023
    Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Spiers Memorial Lecture: Analysis andFaraday discussions · 2021
    Article

44 more citing papers are in PubMed but not listed here.

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

8 authors.

Sungwook ChoiDepartment of Biochemistry, University of Pennsylvania, 1009 Stellar Chance Laboratories, 36th and Hamilton Walk, Philadelphia, PA 19104, USA.
Andre Isaacs
Dylan Clements
Dahui Liu
Hyemin Kim
Richard W Scott
Jeffrey D Winkler
William F DeGrado

Funding

De novo design of alpha-helical bundlesR37GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2004 to 2013
$3.6M
Design and mechanistic studies of mimics of antimicrobial peptidesR01AI074866 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2008 to 2012
$3.0M
DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
Design and mechanistic studies of mimics of antimicrobial peptidesR56AI074866 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DEGRADO, WILLIAM · 2013 to 2013
$573k
NIAID NIH HHS AI74866NIAID NIH HHS R01 AI074866NIAID NIH HHS R56 AI074866NIGMS NIH HHS GM54616NIGMS NIH HHS R01 GM054616NIGMS NIH HHS R37 GM054616
6 · The paper itself

Abstract

The emergence of drug-resistant bacteria has compromised the use of many conventional antibiotics, leading to heightened interest in a variety of antimicrobial peptides. Although these peptides have attractive potential as antibiotics, their size, stability, tissue distribution, and toxicity have hampered attempts to harness these capabilities. To address such issues, we have developed small (molecular mass <1,000 Da) arylamide foldamers that mimic antimicrobial peptides. Hydrogen-bonded restraints in the arylamide template rigidify the conformation via hydrogen bond formation and increase activity toward Staphylococcus aureus and Escherichia coli. The designed foldamers are highly active against S. aureus in an animal model. These results demonstrate the application of foldamer templates as therapeutics.

Indexed as

Drug DesignAmidesAnimalsAnti-Bacterial AgentsCell LineCell SurvivalErythrocytesHemolysisHumansMiceMicrobial ViabilityModels, MolecularMolecular ConformationAmidesAnti-Bacterial Agents

Identifiers

PMID19359494
PMCPMC2667368

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.