Influenza is an enveloped virus, consisting of two surface glycoproteins, neuraminidase and hemagglutinin. The viral receptor is a glycoconjugate on which sialic acid is the terminal sugar. Neuraminidase catalyses the cleavage of the terminal sialic acid from the adjoining carbohydrate moiety, thereby assisting the virus to spread, and infect new cells. Thus development of neuraminidase inhibitors has been of great interest. Our studies are based on synthesis of new potential neuraminidase inhibitors. The synthetic strategy that was adopted for the preparation of the potential inhibitors, required the introduction of glycine ethyl ester at C1 of 1,4-lactone derivatives of N-acetylneuraminic acid. Furthermore, the rate of the ring opening of the 1,4-lactones was studied via proton NMR. Structural determination of the lactones are reported using specialized NMR techniques (Inverse Detected Single Quantum Filtered Long Range Spectroscopy). Conformational studies of the lactones were also determined with computational models.
| Identifer | oai:union.ndltd.org:arizona.edu/oai:arizona.openrepository.com:10150/291545 |
| Date | January 1996 |
| Creators | Mamuya, Nellie |
| Contributors | Gervay, Jacquelyn |
| Publisher | The University of Arizona. |
| Source Sets | University of Arizona |
| Language | en_US |
| Detected Language | English |
| Type | text, Thesis-Reproduction (electronic) |
| Rights | Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author. |
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