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. 2022 Sep 8;13:920541. doi: 10.3389/fendo.2022.920541

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Copyright © 2022 Lisco, De Tullio, Disoteo, De Geronimo, Piazzolla, De Pergola, Giagulli, Jirillo, Guastamacchia, Sabbà and Triggiani

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Tirzepatide primary structure. TZP is a 39-peptide containing different native and not-native incretins fragments, including GIP, GIP, GLP-1, and Extendin-4 (and glucagon, not shared). Alpha aminobutyric acid is placed in positions 2 and 13 and provides TZP an intrinsic resistance to DPP-IV attack and more structural stability, respectively. A 20-carbon fatty acid, namely eicosanedioic acid, is linked to Glu. A 2xAdo unit is attached to the lysine residue in position 20 and allows TZP to be bound to albumin, consequently increasing its half-life to five days. It is currently debated whether the acylation may also increase receptor bounding stability, hypothetically affecting the pharmacological potency of TZP.