Evidence map›Paper›PMID 37548712›Full record

ArticleAmino acids2023

Purification, conformational analysis and cytotoxic activities of host-defense peptides from the Tungara frog Engystomops pustulosus (Leptodactylidae; Leiuperinae).

J Michael Conlon, Laure Guilhaudis, Samir Attoub, Laurent Coquet, Jérôme Leprince, Thierry Jouenne, Milena Mechkarska

Abstract read
In one paragraph

Article in Amino acids, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Skin secretions of Leptodactylidae (Anura) and their potential applications.The journal of venomous animals and toxins including tropical diseases · 2024
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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.

J Michael ConlonDiabetes Research Centre, School of Biomedical Sciences, Ulster University, Coleraine, BT52 1SA, Northern Ireland, UK. jmconlon1@gmail.com.
Laure GuilhaudisLaboratoire COBRA (UMR 6014 & FR 3038), INSA de Rouen, CNRS, Université Rouen Normandie, 76000, Rouen, France.
Samir AttoubDepartment of Pharmacology and Therapeutics, College of Medicine and Health Sciences, United Arab Emirates University, 17666, Al Ain, United Arab Emirates.
Laurent CoquetCNRS UAR2026, HeRacLeS-PISSARO PBS UMR 6270, Université Rouen Normandie, 76000, Rouen, France.
Jérôme LeprinceCNRS UAR2026, HeRacLeS-PISSARO PBS UMR 6270, Université Rouen Normandie, 76000, Rouen, France.
Thierry JouenneCNRS UAR2026, HeRacLeS-PISSARO PBS UMR 6270, Université Rouen Normandie, 76000, Rouen, France.
Milena MechkarskaDepartment of Life Sciences, Faculty of Science and Technology, The University of The West Indies, St. Augustine Campus, St. Augustine, Trinidad and Tobago.

Funding

Carnot institute 12CLabex SynOrg ANR-11-LABX-0029UWI Campus Research and Publication Fund CRP.3.NOV16.8(1)
6 · The paper itself

Abstract

The amphibian family Leptodactylidae is divided into three sub-families: Leiuperinae, Leptodactylinae, and Paratelmatobiinae. Host-defense peptides (HDPs) present in the skins of frogs belonging to the Leptodactylinae have been studied extensively, but information is limited  regarding peptides from Leiuperinae species. Peptidomic analysis of norepinephrine-stimulated skin secretions from the Tungara frog Engystomops pustulosus (Leiuperinae) collected in Trinidad led to the isolation and structural characterization of previously undescribed pustulosin-1 (FWKADVKEIG KKLAAKLAEELAKKLGEQ), [Q28E] pustulosin-1 (pustulosin-2), and pustulosin-3 (DWKETAKELLKKIGAKVAQVISDKLNPAPQ). The primary structures of these peptides do not resemble those of previously described frog skin HDPs. In addition, the secretions contained tigerinin-1EP (GCKTYLIEPPVCT) with structural similarity to the tigerinins previously identified in skin secretions from frogs from the family Dicroglossidae. Pustulosin-1 and -3 adopted extended α-helical conformations in 25% trifluoroethanol-water and in the presence of cell membrane models (sodium dodecylsulfate and dodecylphosphocholine micelles). Pustulosin-1 and -3 displayed cytotoxic activity against a range of human tumor-derived cell lines (A549, MDA-MB-231, and HT29), but their therapeutic potential for development into anti-cancer agents is limited by their comparable cytotoxic activity against non-neoplastic human umbilical vein endothelial cells. The peptides also displayed weak antimicrobial activity against Escherichia coli (MIC = 125 µM) but were inactive against Staphylococcus aureus. Tigerinin-1EP was inactive against both the tumor-derived cells and bacteria.

Indexed as

Antineoplastic AgentsNeoplasmsAmphibian ProteinsAnimalsAntimicrobial Cationic PeptidesAnuraEndothelial CellsHumansMicrobial Sensitivity TestsSkinAmphibian ProteinsAntimicrobial Cationic PeptidesAntineoplastic AgentsCytotoxicFrog skinHost-defense peptidePustulosinTigerinin

Identifiers

PMID37548712
PMCPMC10689532

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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.