ArticleActa pharmaceutica Sinica. B2021
Facile synthesis of insulin fusion derivatives through sortase A ligation.
Article in Acta pharmaceutica Sinica. B, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 13 citations in OpenAlex.
- Modulation of insulin receptor activation through controlled folding of peptide ligands.Organic & biomolecular chemistry · 2025Article
- Sortase-mediated labeling: Expanding frontiers in site-specific protein functionalization opens new research avenues.Current opinion in chemical biology · 2024Review
- Synthesis and Characterization of Phenylboronic Acid-Modified Insulin With Glucose-Dependent Solubility.Frontiers in chemistry · 2022Article
- Editorial of Special Column "Novel Peptides and Peptidomimetics in Drug Discovery".Acta pharmaceutica Sinica. B · 2021Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Insulin derivatives such as insulin detemir and insulin degludec are U.S. Food and Drug Administration (FDA)-approved long-acting insulin currently used by millions of people with diabetes. These derivatives are modified in C-terminal B29 lysine to retain insulin bioactivity. New and efficient methods for facile synthesis of insulin derivatives may lead to new discovery of therapeutic insulin. Herein, we report a new method using sortase A (SrtA)-mediated ligation for the synthesis of insulin derivatives with high efficiency and functional group tolerance in the C-terminal B chain. This new insulin molecule (Ins-SA) with an SrtA-recognizing motif can be conjugated to diverse groups with N-terminal oligoglycines to generate new insulin derivatives. We further demonstrated that a new insulin derivative synthesized by this SrtA-mediated ligation shows strong cellular and
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