ArticleJournal of peptide science : an official publication of the European Peptide Society2016
Removal of the 5-nitro-2-pyridine-sulfenyl protecting group from selenocysteine and cysteine by ascorbolysis.
Article in Journal of peptide science : an official publication of the European Peptide Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 19 citations in OpenAlex.
- New Role for Radical SAM Enzymes in the Biosynthesis of Thio(seleno)oxazole RiPP Natural Products.Biochemistry · 2021Article
- Chemistry and Chemical Biology of Selenenyl Sulfides and Thioseleninic Acids.Antioxidants & redox signaling · 2020Article
- 2,2'-Dipyridyl diselenide: A chemoselective tool for cysteine deprotection and disulfide bond formation.Journal of peptide science : an official publication of the European Peptide Society · 2020Article
- Facile removal of 4-methoxybenzyl protecting group from selenocysteine.Journal of peptide science : an official publication of the European Peptide Society · 2019Article
- Diselenide-selenoester ligation for chemical protein synthesis.Nature protocols · 2019Article
- Synthesis of alpha-methyl selenocysteine and its utilization as a glutathione peroxidase mimic.Journal of peptide science : an official publication of the European Peptide Society · 2019Article
- Can dimedone be used to study selenoproteins? An investigation into the reactivity of dimedone toward oxidized forms of selenocysteine.Protein science : a publication of the Protein Society · 2019Article
- Synthesis and semisynthesis of selenopeptides and selenoproteins.Current opinion in chemical biology · 2018Review
- Chemical synthesis of membrane proteins: a model study on the influenza virus B proton channel.Chemical science · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
We previously reported on a method for the facile removal of 4-methoxybenzyl and acetamidomethyl protecting groups from cysteine (Cys) and selenocysteine (Sec) using 2,2'-dithiobis-5-nitropyridine dissolved in trifluoroacetic acid, with or without thioanisole. The use of this reaction mixture removes the protecting group and replaces it with a 2-thio(5-nitropyridyl) (5-Npys) group. This results in either a mixed selenosulfide bond or disulfide bond (depending on the use of Sec or Cys), which can subsequently be reduced by thiolysis. A major disadvantage of thiolysis is that excess thiol must be used to drive the reaction to completion and then removed before using the Cys-containing or Sec-containing peptide in further applications. Here, we report a further advancement of this method as we have found that ascorbate at pH 4.5 and 25 °C will reduce the selenosulfide to the selenol. Ascorbolysis of the mixed disulfide between Cys and 5-Npys is much less efficient but can be accomplished at higher concentrations of ascorbate at pH 7 and 37 °C with extended reaction times. We envision that our improved method will allow for in situ reactions with alkylating agents and electrophiles without the need for further purification, as well as a number of other applications. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.
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