Issue October 2004

category image Volume 22
No. 2 (p 119-252)
October 2004
ISSN 0739-110

Interactions of 5-deazapteridine Derivatives with Mycobacterium tuberculosis and with Human Dihydrofolate Reductases (p. 119-130)

There are major differences between the structures of human dihydrofolate reductase (hDHFR) and Mycobacterium tuberculosis dihydrofolate reductase (mtDHFR). These differences may allow us to design more selective mtDHFR inhibitors. In this paper we study the reactions of six different compounds derived from 5-deazapteridine with human and bacterial enzymes. Results suggest that the addition of hydrophobic groups to the aminophenyl ring would increase mtDHFR-inhibitor affinity and selectivity.

Key words: Mycobacterium tuberculosis, DHFR, Simulation study, Docking.

Elaine F. F. da Cunha1*
Teodorico de Castro Ramalho2
Ricardo Bicca de Alencastro1
Elaine Rose Maia3

1Instituto de Quimica da Universidade Federal do Rio de Janeiro ? UFRJ
Departamento de Quimica Organica
Centro de Tecnologia-Bl A-Sala 609
Ilha do Fundao, Rio de Janeiro
CEP 21949-900 - RJ ? Brazil
2Departamento de Quimica
Instituto Militar de Engenharia
Praca General Tiburcio 80
Urca, Rio de Janeiro
CEP 22290-270 - RJ ? Brazil
3LEEM Fisico-Quimica
Instituto de Quimica
Universidade de Brasilia
Cidade Universitaria
Campus Darcy Ribeiro, Brasilia
CEP 70919-970 - DF ? Brazil
*elaine@iq.ufrj.br

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