Persistent Link:
http://hdl.handle.net/10150/291545
Title:
Synthesis and NMR studies of neuraminidase inhibitors
Author:
Mamuya, Nellie
Issue Date:
1996
Publisher:
The University of Arizona.
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.
Abstract:
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.
Type:
text; Thesis-Reproduction (electronic)
Keywords:
Chemistry, Organic.; Chemistry, Pharmaceutical.
Degree Name:
M.S.
Degree Level:
masters
Degree Program:
Graduate College; Chemistry
Degree Grantor:
University of Arizona
Advisor:
Gervay, Jacquelyn

Full metadata record

DC FieldValue Language
dc.language.isoen_USen_US
dc.titleSynthesis and NMR studies of neuraminidase inhibitorsen_US
dc.creatorMamuya, Nellieen_US
dc.contributor.authorMamuya, Nellieen_US
dc.date.issued1996en_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © 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.en_US
dc.description.abstractInfluenza 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.en_US
dc.typetexten_US
dc.typeThesis-Reproduction (electronic)en_US
dc.subjectChemistry, Organic.en_US
dc.subjectChemistry, Pharmaceutical.en_US
thesis.degree.nameM.S.en_US
thesis.degree.levelmastersen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.disciplineChemistryen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorGervay, Jacquelynen_US
dc.identifier.proquest1383559en_US
dc.identifier.bibrecord.b34507383en_US
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