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Moon et al suggested a hypothesis that GLP-1 Thr 13 interacts with a binding pocket formed by Ile 196 , Leu 232 , and Met 233 of GLP-1R because Thr 7 -containing chimeric peptides are highly sensitive for the Ile 196 mutation;24 but it contradicts the model constructed by Zhang et al that Lys 197 of GLP-1R is highly conserved and is hydrogen bonded to Thr 13 of GLP-1.12 The substitution of GLP-1 Thr 13 or GIP Ile 7 with Ala obviously decreased their receptor-activating activities25,26 and the substitution of GIP Ile 7 with Thr decreased its cAMP activity (pEC 50 : 9.769.58;Emax: 9.918.90).23 Incorporating Thr 7 from GLP-1 into tirzepatide may lower its GIP activity slightly

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However, Dihexa remains entirely preclinical, and its foundational research has faced serious integrity concerns including an expression of concern and a retraction on key papers

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