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Selenopeptide chemistry
Author(s) -
Muttenthaler Markus,
Alewood Paul F.
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.1075
Subject(s) - selenocysteine , dehydroalanine , chemistry , cysteine , peptide , amino acid , selenium , native chemical ligation , biochemistry , combinatorial chemistry , organic chemistry , enzyme
This review focuses on the chemical aspects of the 21st proteinogenic amino acid, selenocysteine in peptides and proteins. It describes the physicochemical properties of selenium/sulfur and selenocysteine/cysteine based on comprehensive structural (X‐ray, NMR, CD) and biological data, and illustrates why selenocysteine is considered the most conservative substitution of cysteine. The main focus lies on the synthetic methods on selenocysteine incorporation into peptides and proteins, including an overview of the selenocysteine building block syntheses for Boc‐ and Fmoc‐SPPS. Selenocysteine‐mediated reactions such as native chemical ligation and dehydroalanine formation are addressed towards peptide conjugation. Selenopeptides have very interesting and distinct properties which lead to a diverse range of applications such as structural, functional and mechanistic probes, robust scaffolds, enzymatic reaction design, peptide conjugations and folding tools. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.