One‐Pot Ligation–Oxidative Deselenization at Selenocysteine and Selenocystine
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Open Access
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ArticleAbstract
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.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.
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Date
2016-11-16Publisher
WileyLicence
OtherRights statement
This is the peer reviewed version of the following article: N. J. Mitchell, S. S. Kulkarni, L. R. Malins, S. Wang, R. J. Payne, Chem. Eur. J. 2017 , 23 , 946., which has been published in final form at doi.org/10.1002/chem.201604709. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.Faculty/School
Faculty of ScienceShare