Evidence map›Paper›PMID 31422479›Full record

ArticleJournal of molecular modeling2019

Molecular modeling of four Dermaseptin-related peptides of the gliding tree frog Agalychnis spurrelli.

Sebastián Cuesta, Felipe Gallegos, Josefa Arias, Fernanda Pilaquinga, Ailín Blasco-Zúñiga, Carolina Proaño-Bolaños, Miryan Rivera, Lorena Meneses

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Journal of molecular modeling, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

8 authors at 2 institutions in 1 country.

Sebastián CuestaLaboratorios LIFE, Av. De la Prensa y Juan Galarza, Quito, Ecuador.
Felipe GallegosLaboratorio de Química Computacional, Escuela de Ciencias Químicas, Pontificia Universidad Católica del Ecuador, Av. 12 de Octubre 1076 y Roca, Apartado 17-01-2184, Quito, Ecuador.
Josefa AriasLaboratorio de Química Computacional, Escuela de Ciencias Químicas, Pontificia Universidad Católica del Ecuador, Av. 12 de Octubre 1076 y Roca, Apartado 17-01-2184, Quito, Ecuador.
Fernanda PilaquingaLaboratorio de Química Computacional, Escuela de Ciencias Químicas, Pontificia Universidad Católica del Ecuador, Av. 12 de Octubre 1076 y Roca, Apartado 17-01-2184, Quito, Ecuador.
Ailín Blasco-ZúñigaLaboratorio de Investigación en Citogenética y Biomoléculas de Anfibios-LICBA, Centro de Investigación para la Salud en América Latina-CISeAL, Facultad de Ciencias Exactas y Naturales, Pontificia Universidad Católica del Ecuador, Av. 12 de octubre 1076 y Roca, Apartado 17-01-2184, Quito, Ecuador.
Carolina Proaño-BolañosLaboratorio de Biología Molecular y Bioquímica, Universidad Regional Amazónica Ikiam, Km 7 vía Muyuna, Tena, Ecuador.
Miryan RiveraLaboratorio de Investigación en Citogenética y Biomoléculas de Anfibios-LICBA, Centro de Investigación para la Salud en América Latina-CISeAL, Facultad de Ciencias Exactas y Naturales, Pontificia Universidad Católica del Ecuador, Av. 12 de octubre 1076 y Roca, Apartado 17-01-2184, Quito, Ecuador.
Lorena MenesesLaboratorio de Química Computacional, Escuela de Ciencias Químicas, Pontificia Universidad Católica del Ecuador, Av. 12 de Octubre 1076 y Roca, Apartado 17-01-2184, Quito, Ecuador. lmmeneses@puce.edu.ec.
Pontificia Universidad Católica del Ecuador · ECUniversidad Regional Amazónica IKIAM · EC

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this research, we present a preliminary computational study of four Dermaseptin-related peptides from the skin exudate of the gliding tree frog Agalychnis spurrelli. Experimentally, the amino acid sequence of these peptides was elucidated through molecular cloning and tandem mass spectrometry and synthetic peptides were assayed against E. coli, S. aureus, and C. albicans to determine their antimicrobial properties. With the sequences on hand, a computational study of the structures was carried out, obtaining their physicochemical properties, secondary structure, and their similarity to other known peptides. A molecular docking study of these peptides was also performed against cell membrane and several enzymes are known to be vital for the organisms. Results showed that Dermaseptin-related peptides are α-helical cationic peptides with an isoelectric point above 9.70 and a positive charge of physiological pH. Introducing theses peptides in a database, it was determined that their identity compared with known peptides range from 36 to 82% meaning these four Dermaseptins are novel peptides. This preliminary study of molecular docking suggests the mechanism of action of this peptide is not given by the inhibition of essential enzymatic pathways, but by cell lysis. Graphical abstract.

Indexed as

Molecular Docking SimulationAmphibian ProteinsAnimalsAnti-Infective AgentsAntimicrobial Cationic PeptidesAnuraCandida albicansCloning, MolecularEscherichia coliProtein Structure, SecondaryStaphylococcus aureusAmphibian ProteinsAnti-Infective AgentsAntimicrobial Cationic PeptidesdermaseptinAgalychnis spurrelliAntimicrobial peptidesDermaseptinsMolecular docking

Identifiers

PMID31422479
OpenAlexW2968885476

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.