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Synthesis of therapeutic peptides resistant to degradation by serine proteases

A method to render therapeutic peptides resistant to serine proteases could increase their in vivo stability. The method involves replacing the amino acid adjacent to a serine protease cleavage site with an analog containing a substituted b-carbon during peptide synthesis. Modified versions of glucagon-like peptide-1 (GLP-1), neuropeptide Y (NPY) and other therapeutic peptides incubated with dipeptidyl peptidase-4
(DPP-4; CD26), DPP-8 or other serine proteases had in vitro half-lives at least 10-fold greater than those of the corresponding unmodified peptides. Ongoing work includes testing the modified GLP-1 peptide in animal models of diabetes and metabolic syndrome.
Arisaph Pharmaceuticals Inc. has stabilized GLP-1s in preclinical development to treat diabetes.

SciBX 6(40); doi:10.1038/scibx.2013.1146
Published online Oct. 17, 2013

Patented by the Tufts University School of Medicine; licensed to Arisaph Pharmaceuticals

Heard, K.R. et al. J. Med. Chem.; published online Sept. 17, 2013;
Contact: William W. Bachovchin, Tufts University Sackler School of Graduate Biomedical Sciences, Boston, Mass.