Premium
Front Cover: Basic Amino Acid Conjugates of 1,2‐Diselenan‐4‐amine with Protein Disulfide Isomerase‐like Functions as a Manipulator of Protein Quality Control (Chem. Asian J. 17/2020)
Author(s) -
Tsukagoshi Shunsuke,
Mikami Rumi,
Arai Kenta
Publication year - 2020
Publication title -
chemistry – an asian journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.18
H-Index - 106
eISSN - 1861-471X
pISSN - 1861-4728
DOI - 10.1002/asia.202000830
Subject(s) - protein disulfide isomerase , oxidative folding , protein folding , chemistry , amino acid , folding (dsp implementation) , biochemistry , conjugate , oxidative phosphorylation , disulfide bond , mathematical analysis , mathematics , electrical engineering , engineering
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.