The authors are grateful to the ETH-Zürich and Novartis Pharma AG for support of this work. Fmoc=9-fluorenylmethoxycarbonyl.
Fmoc-Compatible Solid-Phase Peptide Synthesis of Long C-Terminal Peptide Thioesters
Article first published online: 14 SEP 2001
Copyright © 2001 WILEY-VCH Verlag GmbH, Weinheim, Fed. Rep. of Germany
Angewandte Chemie International Edition
Volume 40, Issue 18, pages 3395–3396, September 17, 2001
How to Cite
Sewing, A. and Hilvert, D. (2001), Fmoc-Compatible Solid-Phase Peptide Synthesis of Long C-Terminal Peptide Thioesters . Angew. Chem. Int. Ed., 40: 3395–3396. doi: 10.1002/1521-3773(20010917)40:18<3395::AID-ANIE3395>3.0.CO;2-G
- Issue published online: 14 SEP 2001
- Article first published online: 14 SEP 2001
- Manuscript Received: 6 APR 2001
- peptide fragment condensation;
- peptide thioester;
- solid-phase synthesis
AlMe3 and ethanethiol can be used to cleave peptides directly and efficiently from a variety of commercial resins to give C-terminal thioesters. Successful synthesis of the 37 amino acid long BPTI1–37-SEt, an activated fragment used to prepare bovine pancreatic trypsin inhibitor (BPTI; see formula) by native chemical ligation, shows that even thioesters of long peptides of complex composition are accessible using standard resins and 9-fluorenylmethoxycarbonyl (Fmoc) chemistry.