2021 年 61 巻 6 号 p. 370-373
While irreversible aggregation or amyloid formation of denatured proteins is well known and studied in detail, the reversible oligomerization (RO) states of some monomeric proteins at high temperature have been recently discovered by DSC analysis. In this article, the RO states of horse cytochrome c, a simplified BPTI variants with hydrophobic peptide tag at the C-terminus end, the envelope protein domain 3 from dengue 4 virus, and the third PDZ domain of the PSD95 neuronal protein were reviewed. The hydrophobic interaction in the denatured state is indicated to be the main factor to stabilize RO state, and the significance of RO was discussed as a key process for the kinetics of the irreversible amyloid formation.
