Title

A Divergent Approach to the Preparation of Cysteine and Serine Analogs

Document Type

Article

Publication Date

11-1-2008

Department

Chemistry and Biochemistry

Abstract

Malonate diesters containing a prochiral quaternary carbon have been successfully transformed into analogs of cysteine and serine. The chiral half-esters are obtained in good yield, and enantioselectivity by selective hydrolysis using Pig-Liver Esterase (PLE) as the catalyst. The resulting half-ester intermediates are transformed into alpha(2,2-), beta(2.2-), and beta(3.3)-analogs of cysteine and serine. The methodology described here allows for the preparation of both enantiomers of the amino-acid analogs by selective manipulation of the ester and acid functional I ties. This divergent strategy allows a common synthetic strategy to be used to prepare a variety of unnatural amino-acid classes from a common intermediate which should prove useful in the design of novel peptide libraries. Copyright (C) 2008 European Peptide Society and John Wiley & Sons. Ltd.

Publication Title

Journal of Peptide Science

Volume

14

Issue

11

First Page

1151

Last Page

1162