Evidence map›Paper›PMID 28656524›Full record

ArticleMolecular diversity2017

Identification of potential trypanothione reductase inhibitors among commercially available β-carboline derivatives using chemical space, lead-like and drug-like filters, pharmacophore models and molecular docking.

Jorge Rodríguez-Becerra, Lizethly Cáceres-Jensen, José Hernández-Ramos, Lorena Barrientos

Abstract read
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Article in Molecular diversity, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 44% 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

0 citing papers in PubMed, 7 citations in OpenAlex.

No citing paper in PubMed yet.

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

4 authors at 2 institutions in 1 country.

Jorge Rodríguez-BecerraPhysical and Analytical Chemistry Laboratory, PACHEM, Departament of Chemistry, Basic Science Faculty, Universidad Metropolitana de Ciencias de la Educación, UMCE, Santiago, Chile. jorge.rodriguez@umce.cl.ORCID 0000-0003-1496-8410
Lizethly Cáceres-JensenPhysical and Analytical Chemistry Laboratory, PACHEM, Departament of Chemistry, Basic Science Faculty, Universidad Metropolitana de Ciencias de la Educación, UMCE, Santiago, Chile. lyzethly.caceres@umce.cl.
José Hernández-RamosPhysical and Analytical Chemistry Laboratory, PACHEM, Departament of Chemistry, Basic Science Faculty, Universidad Metropolitana de Ciencias de la Educación, UMCE, Santiago, Chile.
Lorena BarrientosChemistry Faculty, Research Center for Nanotechnology and Advanced Materials, CIEN-UC, Pontificia Universidad Católica de Chile, Vicuña Mackenna 4860, Macul, Santiago, Chile.
Metropolitan University of Educational Sciences · CLPontificia Universidad Católica de Chile · CL

Funding

Comisión Nacional de Investigación Científica y Tecnológica FONDECYT-11100308Comisión Nacional de Investigación Científica y Tecnológica FONDECYT-11110421Dirección de Investigación, Universidad Metropolitana de Ciencias de la Educación (DIUMCE) FIBE 15/10Dirección de Investigación, Universidad Metropolitana de Ciencias de la Educación (DIUMCE) MYS I/26 2013
6 · The paper itself

Abstract

American trypanosomiasis or Chagas disease caused by the protozoan Trypanosoma cruzi (T. cruzi) is an important endemic trypanosomiasis in Central and South America. This disease was considered to be a priority in the global plan to combat neglected tropical diseases, 2008-2015, which indicates that there is an urgent need to develop more effective drugs. The development of new chemotherapeutic agents against Chagas disease can be related to an important biochemical feature of T. cruzi: its redox defense system. This system is based on trypanothione ([Formula: see text],[Formula: see text]-bis(glutathyonil)spermidine) and trypanothione reductase (TR), which are rather unique to trypanosomes and completely absent in mammalian cells. In this regard, tricyclic compounds have been studied extensively due to their ability to inhibit the T. cruzi TR. However, synthetic derivatives of natural products, such as [Formula: see text]-carboline derivatives ([Formula: see text]-CDs), as potential TR inhibitors, has received little attention. This study presents an analysis of the structural and physicochemical properties of commercially available [Formula: see text]-CDs in relation to compounds tested against T. cruzi in previously reported enzymatic assays and shows that [Formula: see text]-CDs cover chemical space that has not been considered for the design of TR inhibitors. Moreover, this study presents a ligand-based approach to discover potential TR inhibitors among commercially available [Formula: see text]-CDs, which could lead to the generation of promising [Formula: see text]-CD candidates.

Indexed as

CarbolinesComputer SimulationDatabases, PharmaceuticalDrug Evaluation, PreclinicalEnzyme InhibitorsGlutathioneModels, MolecularMolecular Docking SimulationMolecular StructureNADH, NADPH OxidoreductasesSpermidineTrypanocidal AgentsTrypanosoma cruziCarbolinesEnzyme InhibitorsGlutathioneNADH, NADPH OxidoreductasesSpermidineTrypanocidal Agentstrypanothionetrypanothione reductase-CarbolineChemical spacePharmacophore modeling and dockingTrypanosoma cruziTrypanothione reductase

Identifiers

PMID28656524
OpenAlexW2724807819

What OpenQuestion holds

Textmetadata
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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.