Redox-active cyclodextrin exhibits excellent chaperone activities during protein folding

https://pubs.rsc.org/en/content/articlelanding/2024/sc/d4sc02123a

A research team from Tokyo University of Agriculture and Technology, Tokushima University, Tohoku University has developed a compound that promotes correct protein folding in a highly concentrated solution. The sulfide-bonds containing cyclodextrin βCDWSH  has binding properties to a variety of proteins and suppresses intermolecular aggregation while promoting the formation of three-dimensional structures, such as the formation of SS bonds.

The research team believes that βCDWSH can be used to manufacture protein and antibody drugs, and to prevent and treat diseases. Regarding disease prevention and treatment, the team believes that βCDWSH may be effective in preventing protein aggregation in the body, as abnormal protein aggregation is thought to be the cause of neurodegenerative diseases such as Alzheimer’s disease.

Redox-active cyclodextrin exhibits excellent chaperone activities during protein folding
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