Please use this identifier to cite or link to this item: 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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