Dissertation/Thesis Abstract

Stereoselective Synthesis of α,α-Disubstituted Amino Acids Utilizing Porcine Liver Esterase and the Petasis Borono-Mannich Reaction
by Guerrera, Cessandra, M.S., Southern Connecticut State University, 2017, 82; 10283110
Abstract (Summary)

Arginase is a manganese-containing enzyme that catalyzes the hydrolysis of L-arginine to yield L-ornithine and urea. It has been suggested that inhibition of arginase could be of therapeutic utility, and an arginase inhibitor is currently in phase I clinical trials for a variety of cancer subtypes. To date, the most promising inhibitors reported in the literature are α,α-disubstituted arginine analogs with a boronic acid warhead in place of the substrate guanidine group. However, the stereoselective approaches reported to date for this class of compounds have significant limitations and novel methods are needed. This research investigates two approaches: a route towards α,α-disubstituted amino acids via the enzyme-catalyzed desymmetrization of a meso diester and the utilization of the Petasis borono-Mannich reaction as an alternate enantioselective route for mono-substituted analogs.

Indexing (document details)
Advisor: Ryder, Todd R.
Commitee: Kearns, James K., Webb, Jeffrey A.
School: Southern Connecticut State University
Department: Chemistry
School Location: United States -- Connecticut
Source: MAI 56/06M(E), Masters Abstracts International
Source Type: DISSERTATION
Subjects: Chemistry, Organic chemistry
Keywords: Amino acid synthesis, Enantioselective route, Petasis borono-mannich reaction, Porcine liver esterase
Publication Number: 10283110
ISBN: 9780355188356
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