Please use this identifier to cite or link to this item: http://repositorio.ufla.br/jspui/handle/1/32805
metadata.artigo.dc.title: Analysis of Coxiela burnetti dihydrofolate reductase via in silico docking with inhibitors and molecular dynamics simulation
metadata.artigo.dc.creator: Souza, Felipe Rodrigues de
Guimarães, Ana Paula
Cuya, Teobaldo
Freitas, Matheus Puggina de
Gonçalves, Arlan da Silva
Forgione, Pat
França, Tanos Celmar Costa
metadata.artigo.dc.subject: Q fever
Coxiella burnetii
Dihydrofolate reductase
Molecular dynamics
Febre Q
Diidrofolato redutase
Dinâmica molecular
metadata.artigo.dc.publisher: Taylor & Francis
metadata.artigo.dc.date.issued: 2017
metadata.artigo.dc.identifier.citation: SOUZA, F. R. de et al. Analysis of Coxiela burnetti dihydrofolate reductase via in silico docking with inhibitors and molecular dynamics simulation. Journal of Biomolecular Structure and Dynamics, New York, v. 35, n. 13, p. 2975-2986, 2017.
metadata.artigo.dc.description.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.
metadata.artigo.dc.identifier.uri: https://www.tandfonline.com/doi/abs/10.1080/07391102.2016.1239550
http://repositorio.ufla.br/jspui/handle/1/32805
metadata.artigo.dc.language: en_US
Appears in Collections:DQI - Artigos publicados em periódicos

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