Title
Transferrin fusion technology : a novel approach to prolonging biological half-life of insulinotropic peptides Transferrin fusion technology : a novel approach to prolonging biological half-life of insulinotropic peptides
Author
Faculty/Department
Faculty of Pharmaceutical, Biomedical and Veterinary Sciences . Biomedical Sciences
Publication type
article
Publication
Baltimore, Md ,
Subject
Pharmacology. Therapy
Source (journal)
The journal of pharmacology and experimental therapeutics. - Baltimore, Md
Volume/pages
334(2010) :3 , p. 682-692
ISSN
0022-3565
ISI
000281114900001
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
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.
E-info
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