Event Title
Synthesis of Rigid Analogs of 3-Iodothyronamine
Presentation Type
Poster/Portfolio
Presenter Major(s)
Biomedical Sciences
Mentor Information
Matthew Hart, hartm@gvsu.edu
Department
Chemistry
Location
Henry Hall Atrium 100
Start Date
13-4-2011 12:00 PM
End Date
13-4-2011 1:00 PM
Keywords
Creativity/ Innovation, Life Science
Abstract
3-Iodothyronamine (T1AM) is a bioactive metabolite of the thyroid hormones, thyroxine (T4) and 3,5,3'-triiodothyroxine (T3). T1AM is a potent activator of the Trace Amine Associated Receptor (TAAR1) in vitro. Physiologically, T1AM rapidly induces responses in opposition to those seen by T3 and T4. Several potent agonists have been identified. However, reported antagonists have been modest at best. Previously, we have reported an interesting regulatory pattern for TAAR1 exhibited by structural mirror images, (R)- and (S)-apomorphine. R(-)-Apomorphine exhibited dose-dependent activation of TAAR1, while S(+)-apomorphine exhibited inhibition. Herein, we present the progress towards the synthesis of a proposed TAAR regulator attempting to mimic the conformationally restricted Apomorphine. Developing these compounds could not only lead to a better understanding of TAAR1 receptor's role in biology, but also to advancements in the treatment of patients with thyroid hormone related diseases.
Synthesis of Rigid Analogs of 3-Iodothyronamine
Henry Hall Atrium 100
3-Iodothyronamine (T1AM) is a bioactive metabolite of the thyroid hormones, thyroxine (T4) and 3,5,3'-triiodothyroxine (T3). T1AM is a potent activator of the Trace Amine Associated Receptor (TAAR1) in vitro. Physiologically, T1AM rapidly induces responses in opposition to those seen by T3 and T4. Several potent agonists have been identified. However, reported antagonists have been modest at best. Previously, we have reported an interesting regulatory pattern for TAAR1 exhibited by structural mirror images, (R)- and (S)-apomorphine. R(-)-Apomorphine exhibited dose-dependent activation of TAAR1, while S(+)-apomorphine exhibited inhibition. Herein, we present the progress towards the synthesis of a proposed TAAR regulator attempting to mimic the conformationally restricted Apomorphine. Developing these compounds could not only lead to a better understanding of TAAR1 receptor's role in biology, but also to advancements in the treatment of patients with thyroid hormone related diseases.