Aklima, Jannatul published the artcileDirect Analysis of Mitochondrial Damage Caused by Misfolded/Destabilized Proteins, Computed Properties of 97-67-6, the main research area is misfolded destabilized protein thermal instability mitochondrial damage cellular homeostasis; dengue envelope protein domain 3; membrane; misfolded protein; mitochondria; thermal instability.
Protein quality control is essential for cellular homeostasis. In this study, we examined the effect of improperly folded proteins that do not form amyloid fibrils on mitochondria, which play important roles in ATP production and cell death. First, we prepared domain 3 of the dengue envelope protein in wild type and four mutants with widely different biophys. properties in misfolded/aggregated or destabilized states. The effects of the different proteins were detected using fluorescence microscopy and Western blotting, which revealed that three of the five proteins disrupted both inner and outer membrane integrity, while the other two proteins, including the wild type, did not. Next, we examined the common characteristics of the proteins that displayed toxicity against mitochondria by measuring oligomer size, molten globule-like properties, and thermal stability. The common feature of all three toxic proteins was thermal instability. Therefore, our data strongly suggest that thermally unstable proteins generated in the cytosol can cause cellular damage by coming into direct contact with mitochondria. More importantly, we revealed that this damage is not amyloid-specific.
International Journal of Molecular Sciences published new progress about Amyloid Role: BSU (Biological Study, Unclassified), BIOL (Biological Study). 97-67-6 belongs to class alcohols-buliding-blocks, name is (S)-2-hydroxysuccinic acid, and the molecular formula is C4H6O5, Computed Properties of 97-67-6.
Referemce:
Alcohol – Wikipedia,
Alcohols – Chemistry LibreTexts