One-pot ligation-oxidative deselenization at selenocysteine and selenocystine

The use of native chemical ligation at selenocysteine (Sec) 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 acc...

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Main Authors: Payne, Richard J., Mitchell, Nicholas J., Kulkarni, Sameer S., Wang, Siyao, Malins, Lara
Format: Article
Published: Wiley 2017
Subjects:
Online Access:https://eprints.nottingham.ac.uk/39311/
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author Payne, Richard J.
Mitchell, Nicholas J.
Kulkarni, Sameer S.
Wang, Siyao
Malins, Lara
author_facet Payne, Richard J.
Mitchell, Nicholas J.
Kulkarni, Sameer S.
Wang, Siyao
Malins, Lara
author_sort Payne, Richard J.
building Nottingham Research Data Repository
collection Online Access
description The use of native chemical ligation at selenocysteine (Sec) 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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spelling nottingham-393112020-05-04T18:30:16Z https://eprints.nottingham.ac.uk/39311/ One-pot ligation-oxidative deselenization at selenocysteine and selenocystine Payne, Richard J. Mitchell, Nicholas J. Kulkarni, Sameer S. Wang, Siyao Malins, Lara The use of native chemical ligation at selenocysteine (Sec) 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. Wiley 2017-01-18 Article PeerReviewed Payne, Richard J., Mitchell, Nicholas J., Kulkarni, Sameer S., Wang, Siyao and Malins, Lara (2017) One-pot ligation-oxidative deselenization at selenocysteine and selenocystine. Chemistry - a European Journal, 23 (4). pp. 946-952. ISSN 1521-3765 Peptides Ligation Oxidative Deselenization Glycopeptides Synthesis http://onlinelibrary.wiley.com/doi/10.1002/chem.201604709/full doi:10.1002/chem.201604709 doi:10.1002/chem.201604709
spellingShingle Peptides
Ligation
Oxidative Deselenization
Glycopeptides
Synthesis
Payne, Richard J.
Mitchell, Nicholas J.
Kulkarni, Sameer S.
Wang, Siyao
Malins, Lara
One-pot ligation-oxidative deselenization at selenocysteine and selenocystine
title One-pot ligation-oxidative deselenization at selenocysteine and selenocystine
title_full One-pot ligation-oxidative deselenization at selenocysteine and selenocystine
title_fullStr One-pot ligation-oxidative deselenization at selenocysteine and selenocystine
title_full_unstemmed One-pot ligation-oxidative deselenization at selenocysteine and selenocystine
title_short One-pot ligation-oxidative deselenization at selenocysteine and selenocystine
title_sort one-pot ligation-oxidative deselenization at selenocysteine and selenocystine
topic Peptides
Ligation
Oxidative Deselenization
Glycopeptides
Synthesis
url https://eprints.nottingham.ac.uk/39311/
https://eprints.nottingham.ac.uk/39311/
https://eprints.nottingham.ac.uk/39311/