This work was supported by a grant-in-aid for creative scientific research from the Japan Society for the Promotion of Science (17GS0420), and in part by a grant-in-aid for scientific research from the Ministry of Education, Sports, Science, and Technology of Japan (20380069). We thank Tokai University for their support with a grant-in-aid for high technology research. We also thank Prof. Hiromichi Nagasawa and Shinji Nagata of Tokyo University for sequence analysis and Tsuyoshi Ohira of Kanagawa University for providing Glu-C. Xaa=any amino acid.
The Mercaptomethyl Group Facilitates an Efficient One-Pot Ligation at Xaa-Ser/Thr for (Glyco)peptide Synthesis†
Article first published online: 7 JUL 2010
Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 49, Issue 31, pages 5318–5321, July 19, 2010
How to Cite
Hojo, H., Ozawa, C., Katayama, H., Ueki, A., Nakahara, Y. and Nakahara, Y. (2010), The Mercaptomethyl Group Facilitates an Efficient One-Pot Ligation at Xaa-Ser/Thr for (Glyco)peptide Synthesis. Angew. Chem. Int. Ed., 49: 5318–5321. doi: 10.1002/anie.201000384
- Issue published online: 16 JUL 2010
- Article first published online: 7 JUL 2010
- Manuscript Received: 22 JAN 2010
- Japan Society for the Promotion of Science. Grant Number: 17GS0420
- Ministry of Education, Sports, Science, and Technology of Japan. Grant Number: 20380069
- peptide thioesters;
- synthetic methods
Going native: A mercaptomethyl group on the side-chain hydroxy group of serine and threonine residues facilitates a native chemical ligation reaction at the Xaa-Ser/Thr site (see scheme; R=H or Me). The intermediate thioester is treated to achieve an S- to N-acyl shift. After ligation, the group is spontaneously removed to obtain the glycopeptide contulakin-G and human calcitonin.