Evidence map›Paper›PMID 29654809›Full record

ArticlePeptides2018

Pituitary adenylate cyclase-activating polypeptide is a potent broad-spectrum antimicrobial peptide: Structure-activity relationships.

Charles G Starr, Jerome L Maderdrut, Jing He, David H Coy, William C Wimley

Abstract read
In one paragraph

Article in Peptides, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

29 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
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  3. Article
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  8. Microorganisms · 2024
    Review
  9. Unraveling the intricate link between cell death and neuroinflammation usingFrontiers in cell and developmental biology · 2024
    Review
  10. Unravelling turbot (Frontiers in immunology · 2024
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. An ancient neuropeptide defends the brain against infection.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  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.

Charles G StarrDepartment of Biochemistry and Molecular Biology, Tulane University School of Medicine, New Orleans, LA, United States.
Jerome L MaderdrutPeptide Research Laboratory, Department of Medicine, Tulane University School of Medicine, New Orleans, LA, United States.
Jing HeDepartment of Biochemistry and Molecular Biology, Tulane University School of Medicine, New Orleans, LA, United States.
David H CoyPeptide Research Laboratory, Department of Medicine, Tulane University School of Medicine, New Orleans, LA, United States.
William C WimleyDepartment of Biochemistry and Molecular Biology, Tulane University School of Medicine, New Orleans, LA, United States. Electronic address: wwimley@tulane.edu.
Tulane University · US

Funding

Spontaneous Membrane Translocating PeptidesR01GM111824 · NIGMS · TULANE UNIVERSITY OF LOUISIANA · PI WIMLEY, WILLIAM C · 2016 to 2019
$1.4M
Molecular evolution of Peptide antibiotics for drug-resistant Gram negative bacteriaR21AI119104 · NIAID · TULANE UNIVERSITY OF LOUISIANA · PI WIMLEY, WILLIAM C · 2015 to 2016
$405k
NIAID NIH HHS R21 AI119104NIGMS NIH HHS R01 GM111824
6 · The paper itself

Abstract

Pituitary adenylate cyclase-activating polypeptide (PACAP) is a naturally occurring cationic peptide with potent immunosuppressant and cytoprotective activities. We now show that full length PACAP38 and to a lesser extent, the truncated form PACAP27, and the closely related vasoactive intestinal peptide (VIP) and secretin had antimicrobial activity against the Gram-negative bacteria Escherichia coli in the radial diffusion assay. PACAP38 was more potent than either the bovine neutrophil antimicrobial peptide indolicidin or the synthetic antimicrobial peptide ARVA against E. coli. PACAP38 also had activity against the Gram-positive bacteria Staphylococcus aureus in the same assay with comparable potency to indolicidin and ARVA. In the more stringent broth dilution assay, PACAP38 had moderate sterilizing activity against E. coli, and potent sterilizing activity against the Gram-negative bacteria Pseudomonas aeruginosa. PACAP27, VIP and secretin were much less active than PACAP38 in this assay. PACAP38 also had some activity against the Gram-positive bacteria Bacillus cereus in the broth dilution assay. Many exopeptidase-resistant analogs of PACAP38, including both receptor agonists and antagonists, had antimicrobial activities equal to, or better than PACAP38, in both assays. PACAP38 made the membranes of E. coli permeable to SYTOX Green, suggesting a classical membrane lytic mechanism. These data suggest that analogs of PACPAP38 with a wide range of useful biological activities can be made by judicious substitutions in the sequence.

Indexed as

Anti-Infective AgentsCell MembraneChromatography, High Pressure LiquidEscherichia coliHemolysisPituitary Adenylate Cyclase-Activating PolypeptideSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationStructure-Activity RelationshipVasoactive Intestinal PeptideAnti-Infective AgentsPituitary Adenylate Cyclase-Activating PolypeptideVasoactive Intestinal PeptideAntibiotic resistanceAntimicrobial peptidesInnate immunityPituitary adenylate cyclase-activating polypeptideVasoactive intestinal peptide

Identifiers

PMID29654809
PMCPMC5982112
OpenAlexW2798077660

What OpenQuestion holds

Textmetadata
LicenceTDM
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.