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One‐Pot Ligation–Oxidative Deselenization at Selenocysteine and Selenocystine
Author(s) -
Mitchell Nicholas J.,
Kulkarni Sameer S.,
Malins Lara R.,
Wang Siyao,
Payne Richard J.
Publication year - 2017
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201604709
Subject(s) - native chemical ligation , selenocysteine , ligation , oxidative phosphorylation , chemistry , chemical ligation , serine , peptide , biochemistry , combinatorial chemistry , cysteine , biology , microbiology and biotechnology , phosphorylation , enzyme
The use of native chemical ligation at selenocysteine (Sec) residues with peptide thioesters and additive‐free selenocystine ligation with peptides bearing phenyl selenoesters, in concert with one‐pot oxidative deselenization chemistry, is described. These approaches provide a simple and rapid method for accessing native peptides with serine in place of Sec at the ligation junction. The efficiency of both variants of the one‐pot ligation–oxidative deselenization chemistry is probed through the synthesis of a MUC5AC‐derived glycopeptide.