ORGN 113 |
| It has been shown that carbinolamides are intermediates in the enzyme-catalyzed synthesis of α-amidated peptides. Although carbinolamides are important intermediates in the production of these hormones, little attention has been given to their mechanisms of reaction in water, and, thus, it is difficult to speculate how their reaction is enzymatically catalyzed. The purpose of the work presented here was to synthesize structural analogs of the biological intermediates and study their mechanism of breakdown in water. α-Hydroxyhippuric acid (1), substrate for the enzyme, provides an easily modified template for the study of the breakdown of this carbinolamide system. By replacing the peptide portion of the enzymatic intermediate with various substituted benzene rings, we can evaluate the effect of varying electron demand on the mechanism of breakdown of carbinolamides to the amide and glyoxylate products as a function of pH. The pH-rate profiles for various aromatic substituted derivatives of 1 will be presented, and the mechanism of the acid, hydroxide and buffer catalyzed reactions discussed. The effect of the substituents on the pKa of the hydroxyl group and on the overall rates of reaction will also be evaluated. |
|
Asymmetric Reactions and Syntheses, Physical Organic Chemistry, Combinatorial Chemistry, Total Synthesis
8:00 PM-10:00 PM, Sunday, 26 March 2006 Georgia World Congress Center -- Ex. Hall B4, Poster
Division of Organic Chemistry |