ORGN 155 |
| Glutamic acid has the ability to demonstrate interesting chemistry and has a role in protein's post translational modifications due to the presence of &alpha- and &gamma-COOH functionality. In this study, we explored its reactivity at these two different functional sites. Herein, we showed that there was facile formation of natural or unnatural peptides when the other -COOH group was protected. However, when both of the -COOH groups were activated simultaneously, we observed that the activated &alpha–COOH underwent peptide coupling while the activated &gamma-COOH exhibited cyclization, consequently yielding pyroglutamic dipeptides. These results were also supported by 2D-NMR studies. These studies were carried out under the able guidance of Prof. A. R. Katritzky. |
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Physical Organic Chemistry, Combinatorial and Process Chemistry, New Reactions and Methodology, Peptides, Proteins and Amino Acids
8:00 PM-10:00 PM, Sunday, April 6, 2008 Morial Convention Center -- Hall A, Poster
Division of Organic Chemistry |