GLPwatch
Glycosylation Improves the Proteolytic Stability of Exenatide.
Bioconjug Chem · 2023
Last updated 2026-05-28Researchers modified the GLP-1 drug exenatide by adding a sugar molecule to its structure. This change made the drug more resistant to breakdown in the body while keeping its ability to control blood sugar at the same level as the original version.
AI summary of the abstract below.
| Journal | Bioconjug Chem, 2023 |
|---|---|
| Citations | 8 |
| Relative citation ratio | 1.02 |
| NIH percentile | 51 |
| Molecules | exenatide |
| Conditions studied | Type 2 Diabetes |
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.
Verbatim abstract via PubMed 37192432 ↗
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