Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/32935
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dc.contributor.authorChandrashekar, Chaitra-
dc.contributor.authorNishiuchi, Yuji-
dc.contributor.authorWhite, Barbara Fam-
dc.contributor.authorArsenakis, Yanni-
dc.contributor.authorLin, Feng-
dc.contributor.authorMcNeill, Samantha M-
dc.contributor.authorZhao, Peishen-
dc.contributor.authorvan Dun, Sam-
dc.contributor.authorKoijen, Anna-
dc.contributor.authorKajihara, Yasuhiro-
dc.contributor.authorWootten, Denise-
dc.contributor.authorvan den Bos, Leendert J-
dc.contributor.authorWade, John D-
dc.contributor.authorHossain, Mohammed Akhter-
dc.date2023-
dc.date.accessioned2023-06-07T02:25:18Z-
dc.date.available2023-06-07T02:25:18Z-
dc.date.issued2023-05-16-
dc.identifier.citationBioconjugate Chemistry 2023-05-16, 34(6)en_US
dc.identifier.issn1520-4812-
dc.identifier.urihttps://ahro.austin.org.au/austinjspui/handle/1/32935-
dc.description.abstractExenatide was the first marketed GLP-1 receptor agonist for the treatment of type 2 diabetes. Modification to the chemical structure or the formulation has the potential to increase the stability of exenatide. We introduced human complex-type sialyloligosaccharide to exenatide at the native Asn28 position. The synthesis was achieved using both solid phase peptide synthesis (SPPS) and Omniligase-1-mediated chemoenzymatic ligation. The results demonstrate that glycosylation increases the proteolytic stability of exenatide while retaining its full biological activity.en_US
dc.language.isoeng-
dc.titleGlycosylation Improves the Proteolytic Stability of Exenatide.en_US
dc.typeJournal Articleen_US
dc.identifier.journaltitleBioconjugate Chemistryen_US
dc.identifier.affiliationThe Florey Institute of Neuroscience and Mental Healthen_US
dc.identifier.affiliationGlyTech, Inc., 134 Chudoji Minamimachi, Kyoto 600-8813, Japanen_US
dc.identifier.affiliationMedicine (University of Melbourne)en_US
dc.identifier.affiliationMonash Institute of Pharmaceutical Sciences, 381 Royal Parade, Parkville, Victoria 3052, Australia.en_US
dc.identifier.affiliationEnzyTag B.V., Daelderweg 9, 6361HK Nuth, The Netherlands.en_US
dc.identifier.affiliationGraduate School of Science, Osaka University, Toyonaka, Osaka 560-0043 Japan.en_US
dc.identifier.affiliationARC Centre for Cryo-Electron Microscopy of Membrane Proteins (CCeMMP), Monash Institute of Pharmaceutical Sciences, Parkville, Victoria 3052, Australia.en_US
dc.identifier.affiliationSchool of Chemistry, Parkville, Victoria 3010, Australia.en_US
dc.identifier.affiliationDepartment of Biochemistry and Pharmacology, The University of Melbourne, Parkville, Victoria 3010, Australia.en_US
dc.identifier.affiliationGraduate School of Science, Tohoku University, Sendai, Miyagi 980-8579, Japan.en_US
dc.identifier.affiliationGeneral Medicineen_US
dc.identifier.doi10.1021/acs.bioconjchem.3c00120en_US
dc.type.contentTexten_US
dc.identifier.orcid0000-0002-0288-5952en_US
dc.identifier.orcid0000-0001-7662-5187en_US
dc.identifier.orcid0000-0001-5735-4924en_US
dc.identifier.orcid0000-0003-0185-0595en_US
dc.identifier.orcid0000-0002-6656-2394en_US
dc.identifier.orcid0000-0003-4563-1642en_US
dc.identifier.orcid0000-0002-1352-6568en_US
dc.identifier.orcid0000-0002-9961-0006en_US
dc.identifier.pubmedid37192432-
item.fulltextNo Fulltext-
item.openairetypeJournal Article-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextnone-
item.languageiso639-1en-
item.cerifentitytypePublications-
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