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https://ahro.austin.org.au/austinjspui/handle/1/32935| Title: | Glycosylation Improves the Proteolytic Stability of Exenatide. | Austin Authors: | Chandrashekar, Chaitra;Nishiuchi, Yuji;White, Barbara Fam;Arsenakis, Yanni;Lin, Feng;McNeill, Samantha M;Zhao, Peishen;van Dun, Sam;Koijen, Anna;Kajihara, Yasuhiro;Wootten, Denise;van den Bos, Leendert J;Wade, John D;Hossain, Mohammed Akhter | Affiliation: | The Florey Institute of Neuroscience and Mental Health GlyTech, Inc., 134 Chudoji Minamimachi, Kyoto 600-8813, Japan Medicine (University of Melbourne) Monash Institute of Pharmaceutical Sciences, 381 Royal Parade, Parkville, Victoria 3052, Australia. EnzyTag B.V., Daelderweg 9, 6361HK Nuth, The Netherlands. Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043 Japan. ARC Centre for Cryo-Electron Microscopy of Membrane Proteins (CCeMMP), Monash Institute of Pharmaceutical Sciences, Parkville, Victoria 3052, Australia. School of Chemistry, Parkville, Victoria 3010, Australia. Department of Biochemistry and Pharmacology, The University of Melbourne, Parkville, Victoria 3010, Australia. Graduate School of Science, Tohoku University, Sendai, Miyagi 980-8579, Japan. General Medicine |
Issue Date: | 16-May-2023 | Date: | 2023 | Publication information: | Bioconjugate Chemistry 2023-05-16, 34(6) | Abstract: | Exenatide 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. | URI: | https://ahro.austin.org.au/austinjspui/handle/1/32935 | DOI: | 10.1021/acs.bioconjchem.3c00120 | ORCID: | 0000-0002-0288-5952 0000-0001-7662-5187 0000-0001-5735-4924 0000-0003-0185-0595 0000-0002-6656-2394 0000-0003-4563-1642 0000-0002-1352-6568 0000-0002-9961-0006 |
Journal: | Bioconjugate Chemistry | PubMed URL: | 37192432 | ISSN: | 1520-4812 | Type: | Journal Article |
| Appears in Collections: | Journal articles |
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