Reagentless Oxidative Folding of Bisulfide-Rich Peptides Catalyzed by an Intramolecular Diselenide

摘要

Disulfide bonds are critical to stabilizing the native structure of many peptides and proteins. These crosslinks are formed during oxidative folding, and machinery to assist formation of the correct cysteine pairings is used by all walks of life, from prokaryotes to humans.However, in the chemical synthesis of disulfide-containing biomolecules alternative methods are employed to arrive at the native disulfide connectivity. and usually involves redox buffers and requires peptide-specific optimization.