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The researchers applied this strategy to the incretin hormone glucagon-like peptide 1 (GLP-1), which stimulates insulin and suppresses glucagon secretion. GLP-1 is inactivated in vivo by dipeptidyl peptidase (DPP-4). The thioamide-substituted version of GLP-1 has a 100x increase in stability and is not significantly disruptive to the protein’s secondary structure or activity in cell-based assays.
Thioamide GLP-1 was shown to be active and modulate glucose levels in mice. Other DPP-4 substrates are involved in the treatment of diabetes, obesity, stress, growth and development, or congestive heart failure; thioamide-stabilized versions of these peptides are being synthesized and tested.