MEDI 68 |
| This presentation will highlight our efforts to develop new classes of inhibitors for the important human PLP-dependent enzyme, cystathionine beta-synthase (CBS). This enzyme is central to the transsulfuration pathway, whereby reduced sulfur equivalents are converted from dietary methionine into usable redox equivalents in the form of glutathione. CBS itself combines L-serine with L-homocysteine to give (L,L)-cystathionine, with release of a molecule of water. Our inhibitor design exploits the latent C2-symmetry inherent in the (L,L)-cystathionine enzymatic reaction product, as indicated in the figure. Streamlined syntheses have been developed for each inhibitor series, via a sequence that features modified Mitsunobu conditions and Grubbs cross metathesis, as key steps.
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Poster Session
7:00 PM-9:00 PM, Sunday, August 19, 2007 BCEC -- Exhibit Hall - B2, Poster
Sci-Mix
Division of Medicinal Chemistry |
