Abstract
Previous work has shown that certain β(3)-peptides can effectively mimic the side chain display of an α-helix and inhibit interactions between proteins, both in vitro and in cultured cells. Here we describe a β(3)-peptide analog of GLP-1, CC-3(Act), that interacts with the GLP-1R extracellular domain (nGLP-1R) in vitro in a manner that competes with exendin-4 and induces GLP-1R-dependent cAMP signaling in cultured CHO-K1 cells expressing GLP-1R.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
CHO Cells
-
Cricetulus
-
Dose-Response Relationship, Drug
-
Glucagon-Like Peptide 1 / analogs & derivatives*
-
Glucagon-Like Peptide 1 / pharmacology
-
Glucagon-Like Peptide-1 Receptor
-
Humans
-
Ligands
-
Models, Molecular
-
Receptors, Glucagon / agonists*
-
Structure-Activity Relationship
Substances
-
GLP1R protein, human
-
Glucagon-Like Peptide-1 Receptor
-
Ligands
-
Receptors, Glucagon
-
Glucagon-Like Peptide 1