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.
| Identifer | oai:union.ndltd.org:uno.edu/oai:scholarworks.uno.edu:td-1249 |
| Date | 04 August 2011 |
| Creators | Dodlapati, Sanjeeva |
| Publisher | ScholarWorks@UNO |
| Source Sets | University of New Orleans |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | University of New Orleans Theses and Dissertations |
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