Title

Synthesis and Analysis of N-Acetylhistidine Ethylamide from N- Acetyl -L- Histidine

Publication Date

2010

Document Type

Project Summary

Degree Name

Master of Science

Department

Analytical Chemistry

First Advisor

Dr. Shelly Kumar

Abstract

Photo oxidation of proteins with light and oxygen has known to cause cross linking in proteins by formation of dimer. This leads to cataract formation in eyes. From twenty amino acids, only some amino acids namely Cysteine, Tryptophan, Histidine, Tyrosine, Lysine are known to get photo oxidized and involved in formation of cross links. The amino acid Cysteine which contains thiol group is known to form cross links through disulphide bonds. But the present study is mainly in finding out cross links in other amino acids. Histidine, one the amino acid is selected for photo oxidation studies. However, searching for relatively few crosslink bonds during photo oxidation of proteins has found quite tedious process for researchers. In the previous studies photo oxidation of N-Acetyl Histidine Ethylamide, a derivative synthesized from N-Acetyl histidine was done in which amine group and the carboxylic acid have been converted in to amide bonds. The photo oxidation of N-Acetyl Histidine Ethylamide mimics the Histidine moiety in proteins. The previous study showed that photo oxidation has resulted in the dimer formation due to the reaction of hydrated Imidazolone with the second molecule of N-Acetyl Histidine Ethylamide. Hence to carry out the photo oxidation process, synthesis of N-Acetyl Histidine Ethylamide has become important. First small scale synthesis was carried to know the process of formation of N-Acetylhistidine Ethylamide. Then large scale synthesis was carried for future photo oxidation and NMR studies.

Comments

The preservation and distribution of student research in the form of capstone project summaries, thesis work, and other student work is an important part of the University Library’s responsibility to conserve and disseminate knowledge created at the University.

This page serves as a record that the University Library has received and is preserving the approved manuscript, but at the time of posting sufficient permissions were unavailable for full-text publication.

Please contact opus@govst.edu for more information.

This document is currently not available here.

Share

COinS