Effect of Carboxyl Group Surface Functionalized Carbon Quantum Dots On Hen Egg White Lysozyme (HEWL) Amyloidogenesis

Abstract

Protein misfolding occur due to the failure in protein quality control mechanism present within the cells. These misfolded proteins undergo self-assemble and turn into fibrillar structures known as amyloid fibrils. Amyloid forming proteins possess high ordered beta sheet structures in back bone and hydrogen bonds help out in making stable interaction with other similar structures. Amyloid formation is considered as main pathological event in the onset of neurodegenerative diseases which include Alzheimer’s disease, Parkinson’s disease, Huntington disease, Type-II diabetes, and others. Amyloid fibrils are formed via intermediate states and process followed by proteins is reported to be nucleated condensation polymerization mechanism and associated with many pathophysiological conditions. Voluminous research is being carried out to find effective therapeutics for amyloidosis. In recent times, carbon quantum dots (CQDs) gained attention of active researchers due to their unique semi-conducting, physio-chemical properties, large surface area to volume ratio, optical properties and bio-compatibility. In the study we have synthesized CQDs using kitchen spice mix and these particles are surface functionalized with Carboxylic group. We have demonstrated the characterization of modified CQDs and their action against in vitro amyloid forming model protein Hen Egg White Lysozyme (HEWL). The results shed some light towards the potential candidature of surface functionalized CQDs as therapeutics against amyloidosis.