Date of Award

Summer 8-4-2011

Degree Type

Thesis-Restricted

Degree Name

M.S.

Degree Program

Chemistry

Department

Chemistry

Major Professor

Wang, Guijun

Second Advisor

Trudell, Mark L.

Third Advisor

Jursic, Branko S.

Abstract

Conformationally constrained bicyclic amino acids are invaluable in the synthesis of natural products and peptidomimetics. Aeruginosins contain novel bicyclic amino acid, 2--‐carboxy--‐6--‐hydroxyl octahydrindole (Choi) as the core structure. Aeruginosins are tetra peptide serine protease inhibitors isolated from marine sponges and cyanobacterial water blooms. Rigid bicyclic amino acid(Choi)is an essential core structure, which strongly influences biological activity of aeruginosin family members. Aeruginosins showed promising inhibitory activity against thrombin, trypsin, and factor VIIa. Thrombin and factor VIIa play a major role in blood clotting cascade; excessive coagulation leads to thrombosis and other cardiovascular diseases. Several research groups have reported a number of synthetic aeruginosin analogs.

In this thesis, some of the synthetic methodologies of bicyclic amino acid core of aeruginosins are presented. Importance of bicyclic amino acids in peptidomimetic synthesis and drug designing is presented. Mainly, syntheses of ring oxygenated Choi analogs starting from glucose and mannose are presented.

Rights

The University of New Orleans and its agents retain the non-exclusive license to archive and make accessible this dissertation or thesis in whole or part in all forms of media, now or hereafter known. The author retains all other ownership rights to the copyright of the thesis or dissertation.

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Chemistry Commons

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