Flavivirus

New dengue fever study results from University of Queensland described

"The fusion process is driven by conformational changes in the E protein and is an essential step in the virus life cycle. In this study, we analyzed the pre-fusion and post-fusion structures of the dengue virus E protein to identify potential novel sites that could bind small molecules, which could interfere with the conformational transitions that mediate the fusion process. We used an in silico virtual screening approach combining three different docking algorithms (DOCK, GOLD and FlexX) to identify compounds that are likely to bind to these sites. Seven structurally diverse molecules were selected to test experimentally for inhibition of dengue virus propagation," wrote R. Yennamalli and colleagues, University of Queensland.

The researchers concluded: "The best compound showed an IC50 in the micromolar range against dengue virus type 2.."

Yennamalli and colleagues published their study in the Journal of Computer - Aided Molecular Design (Identification of novel target sites and an inhibitor of the dengue virus E protein. Journal of Computer - Aided Molecular Design, 2009;23(6):333-341).

For additional information, contact B. Kobe, University of Queensland, School Chemical & Molecular Bioscience, Brisbane, Qld 4072, Australia.

The publisher of the Journal of Computer - Aided Molecular Design can be contacted at: Springer, Van Godewijckstraat 30, 3311 Gz Dordrecht, Netherlands.

Keywords: Australia, Brisbane, Computer-Aided Molecular Design, Dengue Fever, Drug Development, Flavivirus, Pharmaceuticals, Therapy, Treatment, University of Queensland.

This article was prepared by Biotech Business Week editors from staff and other reports. Copyright 2009, Biotech Business Week via NewsRx.com.