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Guimaraes A.P.,Federal University of Viçosa | Guimaraes A.P.,Brazilian Military Institute of Engineering | De Souza F.R.,Brazilian Military Institute of Engineering | Oliveira A.A.,University of Sao Paulo | And 4 more authors.
European Journal of Medicinal Chemistry | Year: 2015

Recently we constructed a homology model of the enzyme thymidylate kinase from Variola virus (VarTMPK) and proposed it as a new target to the drug design against smallpox. In the present work, we used the antivirals cidofovir and acyclovir as reference compounds to choose eleven compounds as leads to the drug design of inhibitors for VarTMPK. Docking and molecular dynamics (MD) studies of the interactions of these compounds inside VarTMPK and human TMPK (HssTMPK) suggest that they compete for the binding region of the substrate and were used to propose the structures of ten new inhibitors for VarTMPK. Further docking and MD simulations of these compounds, inside VarTMPK and HssTMPK, suggest that nine among ten are potential selective inhibitors of VarTMPK. © 2014 Elsevier Masson SAS.


PubMed | Federal University of Rio de Janeiro, Federal Institute of Education Science and Technology of Espirito Santo IFES, Federal University of Viçosa, Brazilian Military Institute of Engineering and 2 more.
Type: | Journal: European journal of medicinal chemistry | Year: 2015

Recently we constructed a homology model of the enzyme thymidylate kinase from Variola virus (VarTMPK) and proposed it as a new target to the drug design against smallpox. In the present work, we used the antivirals cidofovir and acyclovir as reference compounds to choose eleven compounds as leads to the drug design of inhibitors for VarTMPK. Docking and molecular dynamics (MD) studies of the interactions of these compounds inside VarTMPK and human TMPK (HssTMPK) suggest that they compete for the binding region of the substrate and were used to propose the structures of ten new inhibitors for VarTMPK. Further docking and MD simulations of these compounds, inside VarTMPK and HssTMPK, suggest that nine among ten are potential selective inhibitors of VarTMPK.


Giacoppo J.O.S.,Federal University of Lavras | Mancini D.T.,Federal University of Lavras | Guimaraes A.P.,Brazilian Military Institute of Engineering | Goncalves A.S.,Federal Institute of Education Science and Technology of Espirito Santo IFES | And 3 more authors.
European Journal of Medicinal Chemistry | Year: 2014

In the present work, we applied docking and molecular dynamics techniques to study 11 compounds inside the enzymes dihydrofolate reductase (DHFR) from the biological warfare agent Bacillus anthracis (BaDHFR) and Homo sapiens sapiens (HssDHFR). Six of these compounds were selected for a study with the mutant BaF96IDHFR. Our results corroborated with experimental data and allowed the proposition of a new molecule with potential activity and better selectivity for BaDHFR. © 2014 Elsevier Masson SAS. All rights reserved.


Guimaraes A.P.,University of Vic | Guimaraes A.P.,Brazilian Military Institute of Engineering | de Souza F.R.,Brazilian Military Institute of Engineering | Oliveira A.A.,University of Sao Paulo | And 4 more authors.
European Journal of Medicinal Chemistry | Year: 2014

Recently we constructed a homology model of the enzyme thymidylate kinase from Variola virus (VarTMPK) and proposed it as a new target to the drug design against smallpox. In the present work, we used the antivirals cidofovir and acyclovir as reference compounds to choose eleven compounds as leads to the drug design of inhibitors for VarTMPK. Docking and molecular dynamics (MD) studies of the interactions of these compounds inside VarTMPK and human TMPK (. HssTMPK) suggest that they compete for the binding region of the substrate and were used to propose the structures of ten new inhibitors for VarTMPK. Further docking and MD simulations of these compounds, inside VarTMPK and HssTMPK, suggest that nine among ten are potential selective inhibitors of VarTMPK. © 2014 Elsevier Masson SAS.


PubMed | Federal Institute of Education Science and Technology of Espirito Santo IFES, Federal University of Lavras and Brazilian Military Institute of Engineering
Type: | Journal: European journal of medicinal chemistry | Year: 2015

In the present work, we applied docking and molecular dynamics techniques to study 11 compounds inside the enzymes dihydrofolate reductase (DHFR) from the biological warfare agent Bacillus anthracis (BaDHFR) and Homo sapiens sapiens (HssDHFR). Six of these compounds were selected for a study with the mutant BaF96IDHFR. Our results corroborated with experimental data and allowed the proposition of a new molecule with potential activity and better selectivity for BaDHFR.

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