Biology

Inhibition and Overexpression Studies of Lysyl Oxidase

Date of Award

2017

Degree Type

Thesis

Degree Name

Master of Science in Biochemistry & Molecular Biology

Department

Biology

Chief Instructor

Charles E. Jakobsche

Second Reader

Frederick T. Greenaway

Third Reader

Donald E. Spratt

Keywords

Biochemistry, Chemistry

Abstract

Lysyl oxidase (LOX) is a 29 kDa quinone-dependent amine oxidase that catalyzes crosslinking reactions in collagen and elastin in developing extracellular matrix. LOX is a current target of medical research due to its relevance in metastatic tumor progression. LOX is a difficult target to study because current attempts at recombinant expression and purification from natural sources are low yielding, and LOX has low solubility in most aqueous buffers. Hydrazine-containing compounds are known inhibitors of LOX and other quinone-dependent amine oxidases; therefore three novel small molecules and two activity- based molecular probes incorporating the hydrazine functionality were synthesized and tested.

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