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Design of Stapled Oxyntomodulin Analogs Containing Functionalized Biphenyl Cross-Linkers

Yulin Tian^1,2, Huafei Zou³, Peng An^1,2

¹Department of Chemistry, State University of New York at Buffalo, Buffalo, New York 14260, United States.

|December 25, 2018

Abstract:

A panel of three lipid-modified, functionalized biphenyl cross-linkers (fBph) were synthesized and subsequently employed in the preparation of the stapled oxyntomodulin (OXM) analogs. In a luciferase-based reporter assay, these stapled OXM analogs showed varying degree of potency in activating GLP-1R and GCGR, presumably due to the disparate effect of the lipid chains on the local environment close to the ligand-receptor binding interface. In particular, the fBph-1 cross-linked peptide with the lipid chain attached to position-3 of the biphenyl cross-linker exhibited the highest dual agonist activity.

Keywords:

GCGR GLP-1R cross-linker dual agonist oxyntomodulin

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