Chemical synthesis of human trefoil factor 1 (TFF1) and its homodimer provides novel insights into their mechanisms of action. Issue 47 (11th May 2020)

• Record Type: Journal Article
• Authors: Braga Emidio, Nayara; Baik, Hayeon; Lee, David; Stürmer, René; Heuer, Jörn; Elliott, Alysha G.; Blaskovich, Mark A. T.; Haupenthal, Katharina; Tegtmeyer, Nicole; Hoffmann, Werner; Schroeder, Christina I.; Muttenthaler, Markus
• Is Part Of: Chemical communications. Volume 56:Issue 47(2020)
• Page Start: 6420
• Page End: 6423
• Publication Date: 2020-05-11
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/d0cc02321c
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Chemical synthesis of gut peptide TFF1 and its homodimer was achieved by a two-fragment ligation strategy followed by oxidative folding. Abstract : TFF1 is a key peptide for gastrointestinal protection and repair. Its molecular mechanism of action remains poorly understood with synthetic intractability a recognised bottleneck. Here we describe the synthesis of TFF1 and its homodimer and their interactions with mucins and Helicobacter pylori . Synthetic access to TFF1 is an important milestone for probe and therapeutic development.