ORGN 675 |
| Short-chain hydroxyacyl-CoA dehydrogenase/ amyloid-ß binding alcohol dehydrogenase (SCHAD/ABAD) is a multifaceted enzyme playing a role in fatty acid, amino acid and steroid metabolism. Being able to visualize this enzyme's activity is critical to understanding its role in metabolism and disease. We have developed a fluorescent probe that measures SCHAD/ABAD activity in intact human cells through fluorescent microscopy. SCHAD/ABAD, a dehydrogenase, converts alcohols to ketones. Basing our design on one of the natural substrates, 17ß-estradiol, we synthesized a library of 2,6 disubstituted naphthalene alcohols. Oxidation of the alcohol to the ketone results in a change in the electronics of the naphthalene core having a profound effect on the fluorescence of the molecule. In vitro kinetic evaluation of the potential substrates identified probe 1 as the lead reporter for SCHAD/ABAD activity. Utilizing fluorescent microscopy, probe 1 can monitor the activity levels of SCHAD/ABAD present in HEK-293T cells.
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Biologically-Related Molecules and Processes
8:00 AM-12:00 PM, Wednesday, August 22, 2007 BCEC -- 258B, Oral
Division of Organic Chemistry |
