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Virtual screening, docking, and dynamics of potential new inhibitors of dihydrofolate reductase from Yersinia pestis.

Author(s): Bastos Lda C, de Souza FR, Guimarães AP, Sirouspour M, Cuya Guizado TR, Forgione P, Ramalho TC, França TC

J Biomol Struct Dyn. 2016 Oct;34(10):2184-98 Authors: Bastos Lda C, de Souza FR, Guimarães AP, Sirouspour M, Cuya Guizado TR, Forgione P, Ramalho TC, França TC

Article GUID: 26494420
Docking and molecular dynamics studies of peripheral site ligand-oximes as reactivators of sarin-inhibited human acetylcholinesterase.

Author(s): de Almeida JS, Cuya Guizado TR, Guimarães AP, Ramalho TC, Gonçalves AS, de Koning MC, França TC

J Biomol Struct Dyn. 2016 Dec;34(12):2632-2642 Authors: de Almeida JS, Cuya Guizado TR, Guimarães AP, Ramalho TC, Gonçalves AS, de Koning MC, França TC

Article GUID: 26612005
Mechanistic studies of new oximes reactivators of human butyryl cholinesterase inhibited by cyclosarin and sarin.

Author(s): de Lima WE, Francisco A, da Cunha EF, Radic Z, Taylor P, França TC, Ramalho TC

J Biomol Struct Dyn. 2017 May;35(6):1272-1282 Authors: de Lima WE, Francisco A, da Cunha EF, Radic Z, Taylor P, França TC, Ramalho TC

Article GUID: 27125569
New insights on molecular interactions of organophosphorus pesticides with esterases.

Author(s): Mangas I, Estevez J, Vilanova E, França TC

Toxicology. 2017 Feb 01;376:30-43 Authors: Mangas I, Estevez J, Vilanova E, França TC

Article GUID: 27311923
Analysis of Coxiela burnetti dihydrofolate reductase via in silico docking with inhibitors and molecular dynamics simulation.

Author(s): de Souza FR, Guimarães AP, Cuya T, de Freitas MP, Gonçalves ADS, Forgione P, Costa França TC

J Biomol Struct Dyn. 2017 Oct;35(13):2975-2986 Authors: de Souza FR, Guimarães AP, Cuya T, de Freitas MP, Gonçalves ADS, Forgione P, Costa França TC

Article GUID: 27726597
Title:Analysis of Coxiela burnetti dihydrofolate reductase via in silico docking with inhibitors and molecular dynamics simulation.
Authors:de Souza FR,  Guimarães AP,  Cuya T,  de Freitas MP,  Gonçalves ADS,  Forgione P,  Costa França TC
Link:https://www.ncbi.nlm.nih.gov/pubmed/27726597?dopt=Abstract
Category:J Biomol Struct Dyn
PMID:27726597
Dept Affiliation: CHEMBIOCHEM
1 a Laboratory of Molecular Modeling Applied to Chemical and Biological Defense (LMCBD) , Military Institute of Engineering , Rio de Janeiro , RJ , Brazil.
2 b Department of Chemistry , Federal University of Viçosa , Viçosa , MG , Brazil.
3 c Faculty of Technology , University of the State of Rio de Janeiro , Resende , RJ , Brazil.
4 d Department of Chemistry , Federal University of Lavras , Lavras , MG , Brazil.
5 e Federal Institute of Education , Science and Technology , Vila Velha , ES , Brazil.
6 f Department of Chemistry and Biochemistry , Concordia University , Montreal , Canada.
7 g Faculty of Management and Informatics , University Hradec Kralove , Hradec Kralove , Czech Republic.

Description:

Analysis of Coxiela burnetti dihydrofolate reductase via in silico docking with inhibitors and molecular dynamics simulation.

J Biomol Struct Dyn. 2017 Oct;35(13):2975-2986

Authors: de Souza FR, Guimarães AP, Cuya T, de Freitas MP, Gonçalves ADS, Forgione P, Costa França TC

Abstract

Coxiella burnetii is a gram-negative bacterium able to infect several eukaryotic cells, mainly monocytes and macrophages. It is found widely in nature with ticks, birds, and mammals as major hosts. C. burnetii is also the biological warfare agent that causes Q fever, a disease that has no vaccine or proven chemotherapy available. Considering the current geopolitical context, this fact reinforces the need for discovering new treatments and molecular targets for drug design against C. burnetii. Among the main molecular targets against bacterial diseases reported, the enzyme dihydrofolate reductase (DHFR) has been investigated for several infectious diseases. In the present work, we applied molecular modeling techniques to evaluate the interactions of known DHFR inhibitors in the active sites of human and C. burnetii DHFR (HssDHFR and CbDHFR) in order to investigate their potential as selective inhibitors of CbDHFR. Results showed that most of the ligands studied compete for the binding site of the substrate more effectively than the reference drug trimethoprim. Also the most promising compounds were proposed as leads for the drug design of potential CbDHFR inhibitors.

PMID: 27726597 [PubMed - indexed for MEDLINE]