Abstract
Acceleration and suppression: Protein disulfide isomerase (PDI) controls protein quality by suppressing protein aggregation, as well as catalyzing oxidative protein folding in the cell. Basic amino acid conjugates of 1,2-diselenan-4-amine, which were inspired by the unique chemical properties for the active center in PDI, effectively catalyze oxidative folding and refolding. In addition, the compounds also show a high suppressive ability against protein aggregation. The observed PDI-like functions of the compounds suggest potential applications not only as an accelerator for protein folding but also as a medicine for misfolding diseases caused by insoluble misfolded proteins. More information can be found in the Full Paper by Kenta Arai et al.
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