Date of Award
Spring 5-2013
Degree Type
Honors College Thesis
Department
Chemistry and Biochemistry
First Advisor
Douglas Masterson
Advisor Department
Chemistry and Biochemistry
Abstract
Malaria is a disease of the blood that is caused by a parasite and affects over forty percent of the world population today. This small parasite can be treated in a very short period of time; however, there are many countries that do not have access to advanced medicine. This means that the people infected with this disease will usually die from complications arising from the illness. Malaria is prevalent in tropical and subtropical countries close to the equator where more than half of the world’s population resides. Dominance of malaria in these areas is because of the low economic stability and the tropical areas have the perfect weather conditions for mosquitoes to blossom.
The unnatural peptide made from the pathways described in this paper is common in creating novel peptides. Manipulation of the unnatural peptide glutathione into the (S) configuration should inhibit glutathione reductase. The (R) configuration of glutathione is the natural state; therefore the (S) conformation creates an unnatural peptide. This enzyme inhibitor will allow for the cells to remain in increased oxidative stress state and kill the malaria parasite.
Copyright
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Recommended Citation
McClendon, Sidney L., "Attempt to Synthesize the (S) Enantiomer of a Glutathione Analog to be an Inhibitor of Glutathione Reductase" (2013). Honors Theses. 112.
https://aquila.usm.edu/honors_theses/112