Abstract:
:Glucose-dependent insulinotropic polypeptide is an incretin hormone that stimulates insulin secretion and reduces postprandial glycaemic excursions. The glucose-dependent action of GIP on pancreatic beta-cells has attracted attention towards its exploitation as a potential drug for type 2 diabetes. Use of NMR or X-ray crystallography is vital to determine the three-dimensional structure of the peptide. Therefore, to understand the basic structural requirements for the biological activity of GIP, the solution structure of the major biologically active fragment, GIP(1-30)amide, was investigated by proton NMR spectroscopy and molecular modelling. The structure is characterised by a full length alpha-helical conformation between residues F(6) and A(28). This structural information could play an important role in the design of therapeutic agents based upon GIP receptor agonists.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Alaña I,Hewage CM,Malthouse JP,Parker JC,Gault VA,O'Harte FPdoi
10.1016/j.bbrc.2004.10.033subject
Has Abstractpub_date
2004-12-03 00:00:00pages
281-6issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(04)02341-1journal_volume
325pub_type
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