869646-27-5Relevant articles and documents
Improved synthetic routes to the selenocysteine derivatives useful for Boc-based peptide synthesis with benzylic protection on the selenium atom
Shimodaira, Shingo,Iwaoka, Michio
, p. 260 - 271 (2017/03/09)
Selenocysteine (Sec) derivatives, i.e., Boc-Sec(MBn)-OH (1) and Boc-Sec(MPM)-OH (2), which are useful for chemical synthesis of selenopeptides, were obtained from L-serine in five steps with total yields of 73% and 74%, respectively. The enantiomeric excesses were confirmed to be >99% e.e. by optical resolution using a chiral column on HPLC. On the other hand, for the case of a Fmoc-protected Sec derivative, i.e., Fmoc-Sec(MPM)-OH, similar reactions resulted in low yields and partial racemization taking place. [PRESENTED EQUATION]
A comprehensive one-pot synthesis of protected cysteine and selenocysteine SPPS derivatives
Flemer, Stevenson
, p. 1257 - 1264 (2015/04/14)
A proof-of-principle methodology is presented in which all commercially-available cysteine (Cys) and selenocysteine (Sec) solid phase peptide synthesis (SPPS) derivatives are synthesized in high yield from easily prepared protected dichalcogenide precursors. A Zn-mediated biphasic reduction process applied to a series of four bis-Nα-protected dichalcogenide compounds allows facile conversion to their corresponding thiol and selenol intermediates followed by insitu S- or Se-alkylation with various electrophiles to directly access twenty one known Cys and Sec SPPS derivatives. Most of these derivatives were able to be precipitated in crude form out of petroleum ether in sufficient purity for direct use as peptide building blocks. Subsequent incorporation of these derivatives into peptide models nicely illustrates their viability and applicability toward SPPS.
Strategic use of non-native diselenide bridges to steer oxidative protein folding
Metanis, Norman,Hilvert, Donald
supporting information; experimental part, p. 5585 - 5588 (2012/07/27)
Targeted insertion of a non-native diselenide cross-link into a cysteine-rich protein can be exploited to direct the early stages of oxidative folding so as to avoid accumulation of unproductive intermediates that limit folding efficiency. This simple strategy could facilitate the production of many difficult-to-fold peptides and proteins. Copyright
Synthetic seleno-glutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency
Metanis, Norman,Keinan, Ehud,Dawson, Philip E.
, p. 16684 - 16691 (2007/10/03)
Selenoenzymes have a central role in maintaining cellular redox potential. These enzymes have selenenylsulfide bonds in their active sites that catalyze the reduction of peroxides, sulfoxides, and disulfides. The selenol/disufide exchange reaction is comm
