This work was supported by PICS 4862 (CNRS, CNRST), Institut Pasteur de Lille, Université Lille Nord de France, Cancéropôle Nord Ouest, Région Nord pas de Calais, and European Community.
A One-Pot Three-Segment Ligation Strategy for Protein Chemical Synthesis†
Article first published online: 16 NOV 2011
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 51, Issue 1, pages 209–213, January 2, 2012
How to Cite
Ollivier, N., Vicogne, J., Vallin, A., Drobecq, H., Desmet, R., El Mahdi, O., Leclercq, B., Goormachtigh, G., Fafeur, V. and Melnyk, O. (2012), A One-Pot Three-Segment Ligation Strategy for Protein Chemical Synthesis. Angew. Chem. Int. Ed., 51: 209–213. doi: 10.1002/anie.201105837
- Issue published online: 29 DEC 2011
- Article first published online: 16 NOV 2011
- Manuscript Received: 18 AUG 2011
- growth factors;
- native chemical ligation;
- solid-phase synthesis;
- synthetic methods
Three in one: Native chemical ligation (NCL) and bis(2-sulfanylethyl)amido (SEA) ligation allow the one-pot assembly of three peptide segments in the N-to-C direction. The SEA group (see picture, blue) is switched off by intramolecular disulfide bond formation during NCL. Then, a phosphine switches it on to trigger the second SEA ligation step. The K1 domain of the hepatocyte growth factor was synthesized and found to be biologically active.