Thursday, September 1, 2022

In contrast to conventional studies of amyloidogenic drugs, quercetin accelerates fibrillation of prion protein. (A GOOD thing.)

QUERCETIN

Some highlights regarding Quercetin and amyloids:

Quercetin binding to prion protein is determined, and the network of the binding site at the molecular level is visualized.

In contrast to conventional studies of amyloidogenic drugs, quercetin accelerates fibrillation of prion protein. (A GOOD thing.)

Quercetin turns fibrils into protease-sensitive, structurally loose and non-cytotoxic forms.

Quercetin shows its uniqueness from typical antiamyloidogenic drugs.

Quercetin treatment can disaggregate moPrP (mouse prion) fibrils and lead to the formation of the proteinase-sensitive amorphous aggregates. Furthermore, quercetin-bound fibrils can reduce the membrane disruption of erythrocytes.

Quercetin is distinct from the typical function of antiamyloidogenic drugs that inhibit the formation of amyloid fibrils.

CURCUMIN

Curcumin may be a powerful alloy and “wing man” to Quercetin.

Curcumin alone reduced prion fibril formation significantly.

Curcumin effectively rescues the cells from apoptosis and decreases the ROS level caused by subsequent co-incubation with prion amyloid fibrils.

I believe urgent clinical trials are needed to assess the efficacy of Quercetin and Curcumin as prophylaxis, and treatment of both Acute and Long COVID.

https://www.sciencedirect.com/science/article/pii/S0753332222005662#

https://pubmed.ncbi.nlm.nih.gov/33187342/

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4235698/

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