Evidence map›Paper›PMID 27345756›Full record

ArticleBioorganic & medicinal chemistry2016

Novel drug design for Chagas disease via targeting Trypanosoma cruzi tubulin: Homology modeling and binding pocket prediction on Trypanosoma cruzi tubulin polymerization inhibition by naphthoquinone derivatives.

Charles O Ogindo, Mozna H Khraiwesh, Matthew George, Yakini Brandy, Nailah Brandy, Ayele Gugssa, Mohammad Ashraf, Muneer Abbas, William M Southerland, Clarence M Lee and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Bioorganic & medicinal chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

9 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. 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

12 authors at 1 institution in 1 country.

Charles O OgindoDepartment of Chemistry, Howard University, 525 College Street, NW, Washington, DC 20059, United States.
Mozna H KhraiweshDepartment of Biology, Howard University, 415 College Street, NW, Washington, DC 20059, United States.
Matthew GeorgeDepartment of Biochemistry and Molecular Biology, Howard University, 520 W Street NW, Washington, DC 20059, United States.
Yakini BrandyDepartment of Chemistry, Howard University, 525 College Street, NW, Washington, DC 20059, United States.
Nailah BrandyDepartment of Chemistry, Howard University, 525 College Street, NW, Washington, DC 20059, United States.
Ayele GugssaDepartment of Biology, Howard University, 415 College Street, NW, Washington, DC 20059, United States.
Mohammad AshrafDepartment of Comprehensive Sciences, Howard University, 260 Locker Hall Street, NW, Washington, DC 20059, United States.
Muneer AbbasDepartment of Microbiology, Howard University, 520 W Street NW, Washington, DC 20059, United States; The National Human Genome Center, Howard University, 2041 Georgia Avenue NW, Washington, DC 20060, United States.
William M SoutherlandDepartment of Biochemistry and Molecular Biology, Howard University, 520 W Street NW, Washington, DC 20059, United States.
Clarence M LeeDepartment of Biology, Howard University, 415 College Street, NW, Washington, DC 20059, United States.
Oladapo BakareDepartment of Chemistry, Howard University, 525 College Street, NW, Washington, DC 20059, United States.
Yayin FangDepartment of Biochemistry and Molecular Biology, Howard University, 520 W Street NW, Washington, DC 20059, United States.
Howard University · US

Funding

Maternal Morbidity and Mortality: Risk Factors, Early Detection and Personalized InterventionUL1TR001409 · NCATS · GEORGETOWN UNIVERSITY · PI GONDRE-LEWIS, MARJORIE C, MELLMAN, THOMAS A · 2015 to 2024
$37.8M
PROTEOMICS CORE FACILITYG12MD007597 · NIMHD · HOWARD UNIVERSITY · PI SOUTHERLAND, WILLIAM M. · 2012 to 2018
$14.8M
NCATS NIH HHS UL1 TR001409NIMHD NIH HHS G12 MD007597
6 · The paper itself

Abstract

Chagas disease, also called American trypanosomiasis, is a parasitic disease caused by Trypanosoma cruzi (T. cruzi). Recent findings have underscored the abundance of the causative organism, (T. cruzi), especially in the southern tier states of the US and the risk burden for the rural farming communities there. Due to a lack of safe and effective drugs, there is an urgent need for novel therapeutic options for treating Chagas disease. We report here our first scientific effort to pursue a novel drug design for treating Chagas disease via the targeting of T. cruzi tubulin. First, the anti T. cruzi tubulin activities of five naphthoquinone derivatives were determined and correlated to their anti-trypanosomal activities. The correlation between the ligand activities against the T. cruzi organism and their tubulin inhibitory activities was very strong with a Pearson's r value of 0.88 (P value <0.05), indicating that this class of compounds could inhibit the activity of the trypanosome organism via T. cruzi tubulin polymerization inhibition. Subsequent molecular modeling studies were carried out to understand the mechanisms of the anti-tubulin activities, wherein, the homology model of T. cruzi tubulin dimer was generated and the putative binding site of naphthoquinone derivatives was predicted. The correlation coefficient for ligand anti-tubulin activities and their binding energies at the putative pocket was found to be r=0.79, a high correlation efficiency that was not replicated in contiguous candidate pockets. The homology model of T. cruzi tubulin and the identification of its putative binding site lay a solid ground for further structure based drug design, including molecular docking and pharmacophore analysis. This study presents a new opportunity for designing potent and selective drugs for Chagas disease.

Indexed as

Amino Acid SequenceChagas DiseaseDrug DesignHumansPolymerizationSequence Homology, Amino AcidTrypanocidal AgentsTrypanosoma cruziTubulinTrypanocidal AgentsTubulinBinding site predictionChagas diseaseHomology modelingNaphthoquinone derivativesStructure based drug design (SBDD)Trypanosoma cruziTubulin polymerization inhibition

Identifiers

PMID27345756
PMCPMC4955813
OpenAlexW2425563990

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.