Masters Theses
Abstract
"Glutamic acid (Glu) and aspartic acid (Asp) are dicarboxylic amino acids and are negatively charged at physiological pH. Glutamate is a key molecule in cellular metabolism and serves as metabolic fuel in the body. It is also the most abundant excitatory neurotransmitter in the mammalian nervous system and it is believed to be involved in cognitive functions such learning and memory retention. It has been used in treatments for mental retardation, muscular dystrophy and ulcers. Aspartate plays a crucial role in generating cellular energy, and is involved in the synthesis of other amino acids, such as methionine, lysine and arginine etc. It plays a role in elimination of ammonia from the body and also serves as an excitatory neurotransmitter in the brain. It is useful in treating chronic fatigue and depression.
Glutamate and aspartate oligomers are of potential use as slow-release sources in food and medicinal chemistry. These highly hydrophilic peptides can also be of use as modifiers in inducing change in functional properties of other substances.
The present study was designed to investigate an enzymatic route for synthesis of aspartate and glutamate homo-oligopeptides. Synthesis route involved the use of a readily available proteolytic enzyme papain that has been used for synthesis of non-polar and basic amino acid peptides. Oligomerization efficiency was evaluated in two reaction media; a micro-aqueous triphasic media and a monophasic media. These media are especially attractive because they minimize the secondary and reverse hydrolysis of the acyl-complex and peptides. Amino acid di-ethyl ester hydrochloride was used as the substrate. The synthesized oligopeptides were characterized with Reverse Phase Liquid Chromatography (RPLC) and Electro-spray Ionization Mass Spectrometry (ESI-MS). The results showed that homo-oligopeptides of aspartate and glutamate can be readily synthesized in both reaction media. The overall peptide yield from both amino acids was found to be higher than 80%. ESI-MS analysis revealed that the degree of oligomerization ranged from 2- 7. The dominant peptides were found to be tri-, tetra- and penta-peptides"--Abstract, page iii.
Advisor(s)
Kapila, Shubhender
Committee Member(s)
Nam, Paul Ki-souk
Westenberg, David J.
Department(s)
Chemistry
Degree Name
M.S. in Chemistry
Publisher
University of Missouri--Rolla
Publication Date
Fall 2006
Pagination
xi, 53 pages
Note about bibliography
Includes bibliographical references (pages 46-48)
Rights
© 2006 Hao Wang, All rights reserved.
Document Type
Thesis - Restricted Access
File Type
text
Language
English
Subject Headings
Amino acids -- MetabolismAspartic acidGlutamic acidHigh performance liquid chromatographyOligomersPapain
Thesis Number
T 9094
Print OCLC #
124045397
Recommended Citation
Wang, Hao, "Enzymatic synthesis and characterization of acidic amino acid oligomers" (2006). Masters Theses. 5885.
https://scholarsmine.mst.edu/masters_theses/5885
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