Evidence map›Paper›PMID 15105101›Full record

ArticleAntimicrobial agents and chemotherapy2004

Antibacterial activities of rhodamine B-conjugated gelsolin-derived peptides compared to those of the antimicrobial peptides cathelicidin LL37, magainin II, and melittin.

Robert Bucki, Jennifer J Pastore, Paramjeet Randhawa, Rolands Vegners, Daniel J Weiner, Paul A Janmey

Open access · greenAbstract readComparative Study
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

45 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Targeting Iron - Respiratory Reciprocity Promotes Bacterial Death.bioRxiv : the preprint server for biology · 2024
    Article
  5. Review
  6. Inoculum effect of antimicrobial peptides.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. Review of PIP2 in Cellular Signaling, Functions and Diseases.International journal of molecular sciences · 2020
    Review
  9. Article
  10. Article
  11. Susceptibility of microbial cells to the modified PIPJournal of nanobiotechnology · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. The Role of Cathelicidin LL-37 in Cancer Development.Archivum immunologiae et therapiae experimentalis · 2016
    Review
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

6 authors at 4 institutions in 3 countries.

Robert BuckiDepartment of Physiology and the Institute for Medicine and Engineering, Vagelos Research Laboratories, University of Pennsylvania, Philadelphia 19104, USA. buckirob@mail.med.upenn.edu
Jennifer J Pastore
Paramjeet Randhawa
Rolands Vegners
Daniel J Weiner
Paul A Janmey
University of Pennsylvania · USChildren's Hospital of Philadelphia · USLatvijas Organiskās Sintēzes Institūts · LVMedical University of Białystok · PL

Funding

Novel antibacterial agents resistant to inactivation by polyelectrolytesR01HL067286 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI JANMEY, PAUL A · 2001 to 2010
$2.5M
REVERSIBLE FORMATION AND STRUCTURE OF ACTIN NETWORKSR01AR038910 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI JANMEY, PAUL A · 1991 to 2006
$2.2M
REVERSIBLE FORMATION AND STRUCTURE OF ACTIN NETWORKSR29AR038910 · NIAMS · MASSACHUSETTS GENERAL HOSPITAL · PI JANMEY, PAUL A · 1987 to 1989
–
NHLBI NIH HHS R01 HL067286NHLBI NIH HHS R01 HL67286NIAMS NIH HHS AR38910NIAMS NIH HHS R01 AR038910
6 · The paper itself

Abstract

The growing number of antibiotic-resistant bacteria necessitates the search for new antimicrobial agents and the principles by which they work. We report that cell membrane-permeant rhodamine B (RhB)-conjugated peptides based on the phosphatidylinositol-4,5-bisphosphate binding site of gelsolin can kill the gram-negative organisms Escherichia coli and Pseudomonas aeruginosa and the gram-positive organism Streptococcus pneumoniae. RhB linkage to the QRLFQVKGRR sequence in gelsolin was essential for the antibacterial function, since the unconjugated peptide had no effect on the bacteria tested. Because RhB-QRLFQVKGRR (also termed PBP10), its scrambled sequence (RhB-FRVKLKQGQR), and PBP10 synthesized from D-isomer amino acids show similar antibacterial properties, the physical and chemical properties of these derivatives appear to be more important than specific peptide folding for their antibacterial functions. The similar activities of PBP10 and all-D-amino-acid PBP10 also indicate that a specific interaction between RhB derivatives and bacterial proteins is unlikely to be involved in the bacterial killing function of PBP10. By using a phospholipid monolayer system, we found a positive correlation between the antibacterial function of PBP10, as well as some naturally occurring antibacterial peptides, and the intrinsic surface pressure activity at the hydrophobic-hydrophilic interface. Surprisingly, we observed little or no dependence of the insertion of these peptides into lipid monolayers on the phospholipid composition. These studies show that an effective antimicrobial agent can be produced from a peptide sequence with specificity to a phospholipid not found in bacteria, and comparisons with other antimicrobial agents suggest that the surface activities of these peptides are more important than specific binding to bacterial proteins or lipids for their antimicrobial functions.

Indexed as

Xenopus ProteinsAmino Acid SequenceAntimicrobial Cationic PeptidesBacteriaBinding SitesCathelicidinsEscherichia coliGelsolinHydrogen-Ion ConcentrationLipidsMagaininsMelittenMembranes, ArtificialMicrobial Sensitivity TestsPeptidesPhosphatidylinositol 4,5-DiphosphateAntimicrobial Cationic PeptidesCathelicidinsGelsolinLipidsmagainin 2 peptide, XenopusMagaininsMelittenMembranes, ArtificialPeptidesPhosphatidylinositol 4,5-Diphosphaterhodamine BRhodaminesXenopus Proteins

Identifiers

PMID15105101
PMCPMC400557
OpenAlexW2171544481

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.