Binding modes of two highly potent and non-toxic inhibitors of HIV-1 integrase - 文章详情页

作者：

Zhu, H.M. (Zhu, H.M..) | Chen, W.Z. (Chen, W.Z..) | Wang, C.X. (Wang, C.X..)

收录：

EI Scopus

摘要：

The　complex　structures　of　Human　Immunodeficiency　Virus　Type　1　(HIV-1)　integrase　binding　two　highly　potent　and　non-toxic　inhibitors,　lithospermic　acid　(M522)　and　lithospermic　acid　B　(M532),　were　obtained　using　docking　calculations.　Docking　results　provided　detailed　information　of　their　binding　modes.　The　binding　sites　of　M522　and　M532　were　similar　to　the　inhibitor　5-CITEP.　The　lowest　docking　energies　for　HIV-1　integrase　binding　M522　and　M532　are　in　agreement　with　their　corresponding　lower　IC50　values.　Our　results　on　the　chemical　structure　difference　between　M522　and　M532　show　that　the　carboxyl　and　hydroxyl　groups　on　the　side-chain　of　M532　are　important　chemical　groups　which　could　help　to　increase　the　effect　against　HIV-1　IN　replication.

关键词：

Amino acids Carboxylation DNA Docking Hydroxylation Parameter estimation Proteins Viruses

作者机构：

[ 1 ] [Zhu, H.M.]Coll. of Life Sci. and Bioeng., Beijing University of Technology, Beijing 100022, China
[ 2 ] [Chen, W.Z.]Coll. of Life Sci. and Bioeng., Beijing University of Technology, Beijing 100022, China
[ 3 ] [Wang, C.X.]Coll. of Life Sci. and Bioeng., Beijing University of Technology, Beijing 100022, China

通讯作者信息：

[chen, w.z.]coll. of life sci. and bioeng., beijing university of technology, beijing 100022, china

电子邮件地址：

查看成果更多字段

成果类型
所属机构

所有年份指定年份从至