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dc.contributor.advisorBerkland, Cory J.
dc.contributor.authorAlghaith, Adel Faleh
dc.date.accessioned2012-10-27T10:34:56Z
dc.date.available2012-10-27T10:34:56Z
dc.date.issued2012-08-31
dc.date.submitted2012
dc.identifier.otherhttp://dissertations.umi.com/ku:12309
dc.identifier.urihttp://hdl.handle.net/1808/10211
dc.description.abstractProteins and peptides have been increasingly used to treat many diseases including autoimmune diseases and cancer. The benefits of using peptides and proteins as drugs for treatment are higher target specificity and pharmacological potency when compared to traditional small molecule drugs. However, the instability and immunogenicity of peptides and proteins can limit their translation as therapeutics. Several strategies have been used to improve the physical and chemical stability of peptides and proteins or to extend the half-life in vivo such as modification of N- and C-terminus, PEGylation and cyclization. In addition, glycosylation is a post-traditional modification that can improve the stability of peptides and proteins. Current approaches for synthetic glycosylation often use multiple steps, such as chemical modification of the glycans to form reactive compounds, protection of reactive groups that give undesirable products, using glycosyltransferases to transfer saccharide moieties to peptides and installation of linker molecules to improve reaction efficiency. Two different peptides, aminooxy-proteolipid peptide (AoPLP), and proteolipid peptide (PLP, a known antigen in multiple sclerosis) have been used in this report. A single-step glycosylation in aqueous buffer was achieved by reacting an aminooxy peptide to N-acetyl glucosamine. A series of control experiments suggested that the product formed due to the reaction of the terminal aminooxy group on the peptide with the aldehyde group that is produced from the ring opening of NAG.
dc.format.extent58 pages
dc.language.isoen
dc.publisherUniversity of Kansas
dc.rightsThis item is protected by copyright and unless otherwise specified the copyright of this thesis/dissertation is held by the author.
dc.subjectPharmaceutical sciences
dc.titleA Single-step Reaction for Glycosylation of Aminooxy Peptides
dc.typeThesis
dc.contributor.cmtememberForrest, Laird
dc.contributor.cmtememberVolkin, David B.
dc.thesis.degreeDisciplinePharmaceutical Chemistry
dc.thesis.degreeLevelM.S.
kusw.oastatusna
kusw.oapolicyThis item does not meet KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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