期刊
BIOINFORMATION
卷 4, 期 7, 页码 295-299出版社
BIOMEDICAL INFORMATICS
DOI: 10.6026/97320630004295
关键词
protease; Indinavir; lead expansion; docking; pharmacophore
资金
- DFG [SFB630/C6, Da 208/11-1]
- IZKF (Interdisziplinares Zentrum fur Klinische Forschung der Universitat Wurzburg)
Indinavir (Crivaxan (R)) is a potent inhibitor of the HIV (human immunodeficiency virus) protease. This enzyme has an important role in viral replication and is considered to be very attractive target for new antiretroviral drugs. However, it becomes less effective due to highly resistant new viral strains of HIV, which have multiple mutations in their proteases. For this reason, we used a lead expansion method to create a new set of compounds with a new mode of action to protease binding site. 1300 compounds chemically diverse from the initial hit were generated and screened to determine their ability to interact with protease and establish their QSAR properties. Further computational analyses revealed one unique compound with different protease binding ability from the initial hit and its role for possible new class of protease inhibitors is discussed in this report.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据