Fig. 7: Structure-basis of receptor selectivity demonstrated by tirzepatide, peptide 20 and GLP-1 analogs. | Nature Communications

Fig. 7: Structure-basis of receptor selectivity demonstrated by tirzepatide, peptide 20 and GLP-1 analogs.

From: Structural insights into multiplexed pharmacological actions of tirzepatide and peptide 20 at the GIP, GLP-1 or glucagon receptors

Fig. 7

a Amino acid sequences of endogenous agonists, multi-targeting agonists and approved GLP-1 analogs including semaglutide. Residues are colored according to sequence conservation among GIP, GLP-1 and GCG. Aib, aminoisobutyric acid. Semaglutide and tirzepatide are conjugated by a C20 fatty diacid moiety via a linker connected to the lysine residue at position 20, while peptide 20 is covalently attached by a 16-carbon acyl chain (palmitoyl; 16:0) via a γ-carboxylate spacer at K10P. b Receptor signaling profiles of endogenous agonists, multi-targeting agonists and approved drug GLP-1 analogs including semaglutide. Data shown are means ± S.E.M. of four independent experiments (n = 4) performed in quadruplicate. Source data are provided as a Source Data file. c Receptor binding profiles of endogenous agonists, multi-targeting agonists and approved GLP-1 analogs. Data shown are means ± S.E.M. of three independent experiments (n = 3) performed in duplicate.

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