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. 2009 Jul 14;58(10):2258–2266. doi: 10.2337/db09-0278

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© 2009 by the American Diabetes Association.

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FIG. 1. — Sequence alignment and receptor agonist potencies of OXM and related peptides. A: Sequence alignment of OXM, exendin-4, and related glucagon superfamily peptides including the long acting OXM analogs DualAG and GLPAG. Conserved residues are highlighted. Gln³ is important for GCGR agonist activity. DualAG and GLPAG incorporate a DSer² (S) substitution that confers resistance to DPP-4. The cholesterol moiety (chol) at the C-terminus of these peptides enhances metabolic stability and receptor affinity, and the intervening polyethylene glycol spacer minimizes the loss in agonist potency because of plasma protein/lipid binding. B: In vitro receptor agonist potencies (cAMP release) against mGLP1R and mGCGR and ED₅₀ (nM) in the ex vivo mouse liver glycogenolysis assay (mGlyco). The Gln³→ Glu substitution in GLPAG reduces GCGR agonist activity ∼120- to 400-fold compared with DualAG.