Fully enzymatic N→C-directed peptide synthesis using C-terminal peptide α-carboxamide to ester interconversion

Nuijens, T., Piva, E., Kruijtzer, J.A.W., Rijkers, D.T.S., Liskamp, R.M.J. and Quaedflieg, P.J.L.M. (2011) Fully enzymatic N→C-directed peptide synthesis using C-terminal peptide α-carboxamide to ester interconversion. Advanced Synthesis & Catalysis, 353(7), pp. 1039-1044. (doi:10.1002/adsc.201000943)

Full text not currently available from Enlighten.

Abstract

Chemoenzymatic peptide synthesis is potentially the most cost-efficient technology for the synthesis of short and medium-sized peptides with some important advantages. For instance, stoichiometric amounts of expensive coupling reagents are not required and racemisation does not occur rendering purification easier compared to chemical peptide synthesis. In this paper, a novel interconversion reaction of peptide C-terminal α-carboxamides into primary alkyl esters with alcalase was used to develop a fully enzymatic peptide synthesis strategy. For each elongation step a cost-efficient amino acid carboxamide building block was used followed by the interconversion of the elongated peptide carboxamide to the corresponding primary alkyl ester. These peptide esters are the starting materials for the next enzymatic peptide elongation step.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Liskamp, Professor Robert
Authors: Nuijens, T., Piva, E., Kruijtzer, J.A.W., Rijkers, D.T.S., Liskamp, R.M.J., and Quaedflieg, P.J.L.M.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Advanced Synthesis & Catalysis
ISSN:1615-4150
ISSN (Online):1615-4169

University Staff: Request a correction | Enlighten Editors: Update this record