Evidence map›Paper›PMID 19813703›Full record

ArticleAccounts of chemical research2010

De novo design of antimicrobial polymers, foldamers, and small molecules: from discovery to practical applications.

Gregory N Tew, Richard W Scott, Michael L Klein, William F Degrado

Abstract read
In one paragraph

Article in Accounts of chemical research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 papers.

0numbers the graph read from it
0cells of the map it votes in
142citing papers in PubMed
15.1field-weighted citation impact, top 1% 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

142 citing papers in PubMed, 550 citations in OpenAlex.

  1. Article
  2. Article
  3. Membrane-Focused Strategies AgainstAntibiotics (Basel, Switzerland) · 2026
    Review
  4. Review
  5. Journal of the American Chemical Society · 2026
    Article
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  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Turn-Adopting Peptidomimetic as a Formyl Peptide Receptor-1 Antagonist.ACS pharmacology & translational science · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Article

82 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

4 authors at 1 institution in 1 country.

Gregory N TewDepartment of Chemistry, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6059, USA.
Richard W Scott
Michael L Klein
William F Degrado
University of Pennsylvania · US

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

Antimicrobial peptides (AMPs) provide protection against a variety of pathogenic bacteria and are, therefore, an important part of the innate immune system. Over the past decade, there has been considerable interest in developing AMPs as intravenously administered antibiotics. However, despite extensive efforts in the pharmaceutical and biotechnology industry, it has proven difficult to achieve this goal. While researchers have solved some relatively simple problems such as susceptibility to proteolysis, more severe problems have included the expense of the materials, toxicity, poor efficacy, and limited tissue distribution. In this Account, we describe our efforts to design and synthesize "foldamers"-- short sequence-specific oligomers based on arylamide and beta-amino acid backbones, which fold into well-defined secondary structures-- that could act as antimicrobial agents. We reasoned that small "foldamers" would be less expensive to produce than peptides, and might have better tissue distribution. It should be easier to fine-tune the structures and activities of these molecules to minimize toxicity. Because the activities of many AMPs depends primarily on their overall physicochemical properties rather than the fine details of their precise amino acid sequences, we have designed and synthesized very small "coarse-grained" molecules, which are far simpler than naturally produced AMPs. The molecular design of these foldamers epitomizes the positively charged amphiphilic structures believed to be responsible for the activity of AMPs. The designed oligomers show greater activity than the parent peptides. They have also provided leads for novel small molecule therapeutics that show excellent potency in animal models for multidrug resistant bacterial infections. In addition, such molecules can serve as relatively simple experimental systems for investigations aimed at understanding the mechanism of action for this class of antimicrobial agents. The foldamers' specificity for bacterial membranes relative to mammalian membranes appears to arise from differences in membrane composition and physical properties between these cell types. Furthermore, because experimental coarse-graining provided such outstanding results, we developed computational coarse-grained models to enable molecular dynamic simulations of these molecules with phospholipid membranes. These simulations allow investigation of larger systems for longer times than conventional molecular dynamics simulations, allowing us to investigate how physiologically relevant surface concentrations of AMP mimics affect the bilayer structure and properties. Finally, we apply the principles discovered through this work to the design of inexpensive antimicrobial polymers and materials.

Indexed as

AcrylamidesAmino AcidsAnti-Infective AgentsModels, MolecularMolecular ConformationPolymersAcrylamidesAmino AcidsAnti-Infective AgentsPolymers

Identifiers

PMID19813703
PMCPMC2808429
OpenAlexW2024334224

What OpenQuestion holds

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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.