Date of Award

8-2005

Degree Name

Master of Science

Department

Chemistry

First Advisor

Dr. Brian C. Tripp

Second Advisor

Dr. James Kiddle

Third Advisor

Dr. David Reinhold

Fourth Advisor

Dr. Yirong Mo

Access Setting

Masters Thesis-Open Access

Abstract

Carbonic anhydrase II (CA II) is a zinc metalloenzyme that catalyzes the reversible hydration of carbon dioxide. The role of this reaction in physiology has made it a target of many therapeutic approaches. Most CA II inhibitors currently known are sulfonamide-based and this is the only functional group incorporated into rationally designed CA II inhibitors. Thioxolone (6-hydroxy-1, 3-benzoxathiol-2-one), is a non-sulfonamide that has been found to have CA II inhibitory activity.

Thioxolone and its analogs were studied to evaluate the inhibition activity that can be achieved upon modification of the thioxolone molecule. IC50 values and dissociation constants were determined for thioxolone and its analogs and these were compared to those of potent sulfonamide drugs. Enzyme inhibition kinetics and other spectroscopic methods were used in an attempt to understand the mode of binding of thioxolone to CA II and the mechanism of inhibition. Results indicate a novel binding mode and enhancement of inhibition activity upon structural modification of thioxolone.

Included in

Chemistry Commons

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