The effect of different carbon dots on amyloid aggregation

Many human diseases are associated with misfolding, aggregation and fibril formation of different proteins. For example, amyloid-β in Alzheimer’s disease, α-synuclein in Parkinson`s disease and IAPP in type 2 diabetes are caused by the formation of an insoluble, rich β sheet fibrils of the different proteins. ¹

Polyphenols are a group of natural or synthetic small molecules containing aromatic phenolic rings. Natural polyphenols are a type of phytochemicals which usually uptake in the diet and can be found in various types of food and drinks.^1,2 Different studies have showed that polyphenols can interact with amyloid fibrils, delay and interfere with the fibril formation.^2, It is suggested that the interaction mechanism between the amyloid fibrils and the polyphenols is through aromatic interactions between the phenols rings and the aromatic residues in the protein.²

Carbon quantum dots (C dots) are carbon-based Nano partials with a graphite-based core and an outer layer having functional groups originated from their building blocks reactants. The C dots are of a great interest due to their size (<10nm), their fluorescence emission, biocompatibility and low toxicity.³Recently it was discovered by Jelinek`s lab that L-Lys based C dots can interfere with the aggregation of Prion.³

The aim of this study is to investigate the effect of Tyrosine and Phenylalanine C dots have on IAPP aggregation. The research will focus on the kinetics and morphology aspects of the fibrils formation under the presence and absence of the C dots.