The Effect of Quercetin, Rutin, Morin, and Carmine on Prion Fibrillation In Vitro Approach

Abstract

The conversion of the α-helical, cellular isoform of the prion (PrPC) to the insoluble, β-sheet-rich, infectious, disease-causing isoform (PrPSc) is the fundamental event in the prion diseases which is related Creutzfeldt–Jakob disease. Natural compounds are major sources of small molecule amyloid inhibitors and have been identified with great bioactivities. This study purposed to identify the effects of quercetin, morin, rutin, and carmine as natural compounds on the process of protein fibrillation in a neurodegenerative disease. Thioflavin T (ThT) was used as extrinsic fluorophore on fibrillation detection to determine the effect of bioactive compounds to the fibrillation, followed by Tryptophan as residue that used as intrinsic fluorophore (ITF) and Congo Red as chromophore. This study showed that quercetin has the greatest effect on protein fibrillation both in preincubated and incubated, in ratio 1:5 and 3:5 with around 41% and 44% reduction, respectively, compared to other natural compounds. In conclusion, the role of natural compounds on protein fibrillation showed that quercetin, rutin, morin, and carmine, which have been shown to be effective, may be used in the future development to prevent and disaggregate prion fibrillation in neurodegenerative diseases.