Evidence map›Paper›PMID 17145799›Full record

ArticleAntimicrobial agents and chemotherapy2007

Length effects in antimicrobial peptides of the (RW)n series.

Zhigang Liu, Anna Brady, Anne Young, Brian Rasimick, Kang Chen, Chunhui Zhou, Neville R Kallenbach

Open access · greenAbstract readComparative Study
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

77 citing papers in PubMed, 196 citations in OpenAlex.

  1. Article
  2. Novel Peptide-Triazole Conjugates: Strategic Synthesis, Antimicrobial Properties, and Molecular Docking Study.Journal of peptide science : an official publication of the European Peptide Society · 2026
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  6. From computational screening toFrontiers in microbiology · 2026
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Proline-Modified (RW)ACS omega · 2025
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

17 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

7 authors at 3 institutions in 1 country.

Zhigang LiuDepartment of Chemistry, New York University, 100 Washington Square East, New York, NY 10003, USA.
Anna Brady
Anne Young
Brian Rasimick
Kang Chen
Chunhui Zhou
Neville R Kallenbach
New York University · USEssential Research (United States) · USUniversity of Chicago · US

Funding

SHARED INSTR FACILITIY FOR THE LIFE SCIC06RR016572 · NCRR · NEW YORK UNIVERSITY · PI LENNIE, PETER · 2001 to 2001
$665k
NCRR NIH HHS C06 RR016572NCRR NIH HHS C06 RR-16572
6 · The paper itself

Abstract

A class of antimicrobial peptides involved in host defense consists of sequences rich in Arg and Trp-R and -W. Analysis of the pharmacophore in these peptides revealed that chains as short as trimers of sequences such as WRW and RWR have antimicrobial activity (M. B. Strom, B. E. Haug, M. L. Skar, W. Stensen, T. Stiberg, and J. S. Svendsen, J. Med. Chem. 46:1567-1570, 2003). To evaluate the effect of chain length on antimicrobial activity, we synthesized a series of peptides containing simple sequence repeats, (RW)n-NH2 (where n equals 1, 2, 3, 4, or 5), and determined their antimicrobial and hemolytic activity. The antimicrobial activity of the peptides increases with chain length, as does the hemolysis of red blood cells. Within the experimental error, longer peptides (n equals 3, 4, or 5) show similar values for the ratio of hemolytic activity to antibacterial activity, or the hemolytic index. The (RW)3 represents the optimal chain length in terms of the efficacy of synthesis and selectivity as evaluated by the hemolytic index. Circular dichroism spectroscopy indicates that these short peptides appear to be unfolded in aqueous solution but acquire structure in the presence of phospholipids. Interaction of the peptides with model lipid vesicles was examined using tryptophan fluorescence. The (RW)n peptides preferentially interact with bilayers containing the negatively charged headgroup phosphatidylglycerol relative to those containing a zwitterionic headgroup, phosphatidylcholine.

Indexed as

Anti-Infective AgentsAmino Acid SequenceAnimalsEscherichia coliHemolysisMicrobial Sensitivity TestsMolecular Sequence DataPeptide FragmentsProtein Structure, SecondaryStaphylococcus aureusStructure-Activity RelationshipAnti-Infective AgentsPeptide Fragments

Identifiers

PMID17145799
PMCPMC1797765
OpenAlexW2121654620

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.