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Transferrin fusion technology: a novel approach to prolonging biological half-life of insulinotropic peptides.
- Source :
- The Journal of Pharmacology and Experimental Therapeutics; September 2010, Vol. 334 Issue: 3 p682-692, 11p
- Publication Year :
- 2010
-
Abstract
- Fusion proteins made up of glucagon-like peptide 1 (GLP-1) and exendin-4 (EX-4) fused to a nonglycosylated form of human transferrin (GLP-1-Tf or EX-4-Tf) were produced and characterized. GLP-1-Tf activated the GLP-1 receptor, was resistant to inactivation by peptidases, and had a half-life of approximately 2 days, compared with 1 to 2 min for native GLP-1. GLP-1-Tf retained the acute, glucose-dependent insulin-secretory properties of native GLP-1 in diabetic animals and had a profound effect on proliferation of pancreatic beta-cells. In addition, Tf and the fusion proteins did not cross the blood-brain-barrier but still reduced food intake after peripheral administration. EX-4-Tf proved to be as effective as EX-4 but had longer lived effects on blood glucose and food intake. This novel transferrin fusion technology could improve the pharmacology of various peptides.
Details
- Language :
- English
- ISSN :
- 00223565 and 15210103
- Volume :
- 334
- Issue :
- 3
- Database :
- Supplemental Index
- Journal :
- The Journal of Pharmacology and Experimental Therapeutics
- Publication Type :
- Periodical
- Accession number :
- ejs23378837
- Full Text :
- https://doi.org/10.1124/jpet.110.166470