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Rational Design of an Organometallic Glutathione Transferase Inhibitor
Authors:Wee Han Ang Dr.  Lorien J. Parker  Anastasia De Luca  Lucienne Juillerat‐Jeanneret Dr.  Craig J. Morton Dr.  Mario Lo Bello Prof.  Michael W. Parker Prof.  Paul J. Dyson Prof.
Affiliation:1. Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne (Switzerland);2. Biota Structural Biology Laboratory, St. Vincent's Institute of Medical Research, 9 Princes Street, Fitzroy, Victoria 3065 (Australia);3. Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, 30 Flemington Road, Parkville, Victoria 3010 (Australia);4. Department of Biology, University of Rome Tor Vergata, Via della Ricerca Scientifica snc, Rome 00133 (Italy);5. University Institute of Pathology, Centre Hospitalier Universitaire Vaudois (CHUV), 1011 Lausanne (Switzerland)
Abstract:Double trouble : A hybrid organic–inorganic (organometallic) inhibitor was designed to target glutathione transferases. The metal center is used to direct protein binding, while the organic moiety acts as the active‐site inhibitor (see picture). The mechanism of inhibition was studied using a range of biophysical and biochemical methods.
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Keywords:bioorganometallic chemistry  chemical biology  inhibitors  transferases
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