Modeling HDAC Inhibitors: Structure, Selectivity, and Design
报告人:
Wiest, Olaf
Department of Chemistry & Biochemistry University of Notre Dame
报告时间:
2007-11-21 10:00
报告地点:
生命科学馆143报告厅
主办单位:
清华大学化学系
简介:
Research Description Physical and Theoretical Organic Chemistry, Electron Transfer Induced Processes, Computer Aided Molecular Design Prof. Wiest uses a close connection of computational chemistry and experimental methods to elucidate the mechanisms and transition structures of the transfer of an electron in organic chemistry and biochemically important reactions. Using different electronic structure methods as well as docking and MD techniques, the Wiest group investigated the physical basis for substrate recognition by CPD photolyase and developed a model of the enzyme-substrate complex that was widely recognized and is the current working hypothesis in the community. Prof. Wiest is also interested in applying various computational chemistry techniques to facilitate the molecular design of biologically important agents. Histone deacetylases (HDACs) are key enzymes for chromatin remodeling and the regulation of gene expression. Inhibitors of HDACs are of considerable interest for the treatment of cancer, cystic fibrosis and a variety of other diseases, as demonstrated for example by the FDA approval of SAHA (Zolinza?) in late 2006. The Wiest group at the University of Notre Dame is one of the few groups worldwide with extensive experience in all aspects on computer aided molecular design of HDAC inhibitors
