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The Redox Potential of Selenocystine in Unconstrained Cyclic Peptides
Author(s) -
Besse Dörthe,
Siedler Frank,
Diercks Tammo,
Kessler Horst,
Moroder Luis
Publication year - 1997
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199708831
Subject(s) - dithiothreitol , peptide , chemistry , glutaredoxin , redox , combinatorial chemistry , cyclic peptide , recombinant dna , folding (dsp implementation) , oxidative folding , biochemistry , cysteine , thioredoxin , oxidative stress , enzyme , organic chemistry , engineering , electrical engineering , gene
A much lower redox potential than that of the mixed Sec,Cys‐peptide and particularly of the related Cys,Cys‐peptide is a feature of the cyclic selenocystine‐peptide (Sec,Sec‐peptide). These findings that were obtained with appropriately modified glutaredoxin‐octapeptides at pH 7 [Eq. (1); X = S, Se; DTT = dithiothreitol], open interesting new approaches for the design of productive intermediates in the oxidative folding of synthetic peptides and recombinant proteins. Moreover, such seleno derivatives may represent useful heavy metal analogs for X‐ray structure analysis.