Removal of the 5‐nitro‐2‐pyridine‐sulfenyl protecting group from selenocysteine and cysteine by ascorbolysis

@article{SteMarie2016RemovalOT,
  title={Removal of the 5‐nitro‐2‐pyridine‐sulfenyl protecting group from selenocysteine and cysteine by ascorbolysis},
  author={Emma J Ste Marie and Erik L. Ruggles and Robert J. Hondal},
  journal={Journal of Peptide Science},
  year={2016},
  volume={22},
  pages={571 - 576}
}
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… 
Facile removal of 4‐methoxybenzyl protecting group from selenocysteine
TLDR
It is envisioned that this new method will allow for a simple and gentle “one‐pot” deprotection of Sec(Mob) following solid‐phase peptide synthesis and will minimize the need for extensive purification steps.
2,2′‐Dipyridyl diselenide: A chemoselective tool for cysteine deprotection and disulfide bond formation
  • Emma J Ste Marie, R. Hondal
  • Chemistry, Medicine
    Journal of peptide science : an official publication of the European Peptide Society
  • 2019
TLDR
This work shows the utilization of 2,2′‐dipyridyl diselenide (PySeSePy) as a chemical tool for the removal of Cys‐protecting groups and regioselective formation of disulfide bonds in peptides, and develops a one‐pot method for concomitant deprotection and disulfides bond formation in Cys(Acm) pairs in the presence of an existingDisulfide bond.
Synthesis of alpha‐methyl selenocysteine and its utilization as a glutathione peroxidase mimic
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This work presents a new strategy for the synthesis of (αMe)Sec by alkylation of an achiral methyl malonate through the use of a selenium‐containing alkylating agent synthesized in the presence of dichloromethane and synthesized two peptides: one containing Sec and the other containing (α me)Sec, based on the sequence of glutathione peroxidase.
Can dimedone be used to study selenoproteins? An investigation into the reactivity of dimedone toward oxidized forms of selenocysteine
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It is concluded that dimedone is not a good reagent for detecting selenenic acids in selenoproteins because of the reversible nature of this alkylation.
Chemistry and Chemical Biology of Selenenyl Sulfides (RSeSR) and Thioseleninic acids (RSeSH).
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Diselenide–selenoester ligation for chemical protein synthesis
TLDR
The method’s speed and efficiency may render it useful in the generation of synthetic protein libraries and should find widespread use for the rapid synthesis of proteins, including cases in which other peptide ligation methods cannot be used (or cannot be use efficiently), e.g., at sterically hindered or deactivated acyl donors.
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It is not highly sophisticated, yet the N→S acyl transfer reaction of a native peptide sequence potentially fills an important technology gap. While several routes to synthetic peptide thioesters
Amino acid chalcogen analogues as tools in peptide and protein research
  • L. Moroder, H. Musiol
  • Chemistry, Medicine
    Journal of peptide science : an official publication of the European Peptide Society
  • 2019
TLDR
All of these natural and synthetic chalcogen amino acids have been extensively applied in peptide and protein research to exploit their different physicochemical properties for modulating structural and functional properties in synthetic peptides and rDNA expressed proteins as discussed in the following review.
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