A Cysteine Selenosulfide Redox Switch for Protein Chemical Synthesis

29 November 2019, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


We describe a cyclic selenosulfide derivative of cysteine called SetCys that enables to perform protein chemical synthesis under redox-control.
Native chemical ligation or SEA-mediated ligation with SetCys peptide segments proceeds in a traceless manner and involves the cleavage of a carbon-nitrogen bond in situ.
The manuscript describes detailed mechanistic investigations of SetCys redox-switch and its application to the production of biologically active cyclic protein mimics of hepatocyte growth factor, the high-affinity ligand of MET tyrosine kinase receptor.


cyclic selenosulfide
cysteine surrogate
SEA-mediated reactions
SEA-mediated ligation
Reaction mechanism
Native Chemical Ligation
C-N bond cleavage
Peptide synthesis
Chemical protein synthesis
hepatocyte growth factor
cyclic proteins
tyrosine kinase activity
Cell scattering
AlphaScreen assay
Reaction Kinetic Studies
One-Pot Approach
Redox Switch

Supplementary materials



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