These authors contributed equally to this work.
N-Terminal Protein Modification through a Biomimetic Transamination Reaction†
Article first published online: 17 JUL 2006
Copyright © 2006 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 45, Issue 32, pages 5307–5311, August 11, 2006
How to Cite
Gilmore, J. M., Scheck, R. A., Esser-Kahn, A. P., Joshi, N. S. and Francis, M. B. (2006), N-Terminal Protein Modification through a Biomimetic Transamination Reaction. Angew. Chem. Int. Ed., 45: 5307–5311. doi: 10.1002/anie.200600368
The authors thank the DOE Nanoscale Science and Engineering Technology (NSET) program for financial support, as well as the Department of Chemistry at the University of California, Berkeley, and the Berkeley Chemical Biology Graduate Program. N.S.J. gratefully acknowledges the Saegebarth family for generous fellowship support.
- Issue published online: 7 AUG 2006
- Article first published online: 17 JUL 2006
- Manuscript Revised: 27 MAY 2006
- Manuscript Received: 27 JAN 2006
Vol. 47, Issue 41, 7788, Article first published online: 24 SEP 2008
- bioorganic chemistry;
- protein modifications
One hit wonder: A biomimetic transamination reaction has been developed that employs pyridoxal-5-phosphate to modify the N terminus of proteins and peptides under mild conditions. This technique introduces a uniquely reactive carbonyl group in a single location (see scheme), thus allowing further elaboration through oxime or hydrazone formation. This modification strategy is also compatible with proteins containing a free cysteine residue.