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Synthesis and biodistribution of (C-11) labeled irreversible inhibitors of MAO A and B

Conference · · J. Nucl. Med.; (United States)
OSTI ID:6856685

Alterations in the enzyme monoamine oxidase (MAO) have been implicated in a number of diseases. Two types of MAO (A and B) have been identified by their substrate selectivity as well as their selective inhibition by the propargyl amines clorgyline (la) and L-deprenyl (lb). These inhibitors, which are substrates for MAO A and B respectively, deactivate the enzyme by becoming covalently or irreversibly attached to it, and so, if labeled with a positron emitter may provide selective probes for MAO localization and reactivity in vivo using PET. N-(C-11)methyl 1a and 1b have been synthesized. Synthesis time was 40 min with a radiochemical yield (EOB) of approx. = 20% and a specific activity of approx. = 200 mCi/..mu..mole (EOB). Differences in tissue distribution between control and 1a and 1b in pretreated mice demonstrated specific uptake and retention of each of these tracers to organs known to contain the specific MAO subtype. Centrifugation of brain homogenates showed selective binding of activity to particulate material following protein precipitation. The results support the premise of specific irreversible binding in vivo of 1a to type A and 1b to type B MAO and demonstrate the feasibility of using this approach for probing functional enzyme activity in vivo using PET.

Research Organization:
Chemistry Dept., Brookhaven National Lab., Upton, NY
OSTI ID:
6856685
Report Number(s):
CONF-850611-
Journal Information:
J. Nucl. Med.; (United States), Journal Name: J. Nucl. Med.; (United States) Vol. 26:5; ISSN JNMEA
Country of Publication:
United States
Language:
English

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