Date of Award

5-2023

Degree Type

Thesis

Degree Name

Master of Science (MS)

Department

Chemistry

First Advisor

Benjamin J. Alper, Ph.D.

Abstract

Expre ed in nearly all mammalian tissues, insulin-degrading enzyme (IDE) is a ubiquitous zinc endopeptida e which cleaves many peptides endogenous to human and other organisms. IDE is implicated to hold vital roles in homeostasis, involved in several cellular pathways related to cellular growth, proteasome turnover, and heat- hock respon e. The enzyme also hydrolyzes several ligands of medical interest, such as insulin, amyl in, and amyloid-beta peptide in vivo, and calcitonin, ghrelin, glucagon, and atrial natriuretic peptide in vitro. However, while much is known about the enzyme's function, the mechanism of the IDE cleavage reaction remains poorly understood. The tudy of enzyme inhibition is a vital tool for understanding enzymatic mechanisms of action, and for drug design overall. Here, several new inhibitor of IDE are characterized. These inhibitors belong to a family of broad-spectrum antibiotic commonly used in the field of medicine.

Comments

Master's thesis submitted to the Faculty of the Department of Chemistry at Sacred Heart University in partial fulfillment of the requirements for the degree of Master of Science.

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