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A divergent approach to the preparation of cysteine and serine analogs
Author(s) -
Masterson Douglas S.,
Roy Kinkini,
Rosado Dale A.,
Fouche Marilyn
Publication year - 2008
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1052
Subject(s) - serine , chemistry , cysteine , amino acid , enantiomer , hydrolysis , peptide , combinatorial chemistry , esterase , yield (engineering) , stereochemistry , organic chemistry , biochemistry , enzyme , materials science , metallurgy
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 α 2, 2 ‐, β 2, 2 ‐, and β 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 functionalities. 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 © 2008 European Peptide Society and John Wiley & Sons, Ltd.