Terezie Ticháčková
+420 220 183 339
Další zdroje
Vybrané publikace
Insulin Analogues with Altered Insulin Receptor Isoform Binding Specificities and Enhanced Aggregation Stabilities
Journal of Medicinal Chemistry 64 (19): 14848–14859 (2021)
Insulin is a lifesaver for millions of diabetic patients. There is a need for new insulin analogues with more physiological profiles and analogues that will be thermally more stable than human insulin. Here, we describe the chemical engineering of 48 insulin analogues that were designed to have changed binding specificities toward isoforms A and B of the insulin receptor (IR-A and IR-B). We systematically modified insulin at the C-terminus of the B-chain, at the N-terminus of the A-chain, and at A14 and A18 positions. We discovered an insulin analogue that has Cα-carboxyamidated Glu at B31 and Ala at B29 and that has a more than 3-fold-enhanced binding specificity in favor of the “metabolic” IR-B isoform. The analogue is more resistant to the formation of insulin fibrils at 37 °C and is also more efficient in mice than human insulin. Therefore, [AlaB29,GluB31,amideB31]-insulin may be interesting for further clinical evaluation.
A viral insulin-like peptide inhibits IGF-1 receptor phosphorylation and regulates IGF1R gene expression
Molecular Metabolism 80: 101863 (2024)
Characterization of viral insulins reveals white adipose tissue-specific effects in mice
Molecular Metabolism 44: 101121 (2021)
Nejnovější publikace
A viral insulin-like peptide inhibits IGF-1 receptor phosphorylation and regulates IGF1R gene expression
Molecular Metabolism 80: 101863 (2024)
Insulin Analogues with Altered Insulin Receptor Isoform Binding Specificities and Enhanced Aggregation Stabilities
Journal of Medicinal Chemistry 64 (19): 14848–14859 (2021)
Characterization of viral insulins reveals white adipose tissue-specific effects in mice
Molecular Metabolism 44: 101121 (2021)