Alzheimer’s disease (AD) comes with multifactorial etiologies. Despite copper is present at synaptic junctions, exposure to copper nanoparticles has demonstrated copper's potential roles in AD pathogenesis through beta-amyloid (βA) aggregation. Immuno-spin trapping technique method has demonstrated that βA protein expressing IMR-32 cells or βA protein by themselves can generate radicalized βA proteins after exposure to copper nanoparticles. Despite the available data about the role of nano copper on radical βA protein formation, the mechanism that initiates and promotes the whole process remains unclear. We hypothesized here that critical concentration of protein radical for initiating βA oligomerization is present. The hypothesis was tested by using both pristine form of carbon nanodots (CNDs, a type of quantum dots, specifically U-dots) and organic hybrid form of CNDs in order to balance the radical generating and scavenging power. Copper nanoparticles between 20nm and 80nm sizes were used for exposure to IMR-32 hippocampal neuroblastoma cells expressing βA proteins. Copper nanoparticles of the same size ranges were also used for a direct exposure impact to βA proteins alone. Results indicated that CNDs carries free radical scavening activities and reduced the level of radicalized βA protein concentration. The response pattern of aggregated protein levels after exposure to CNDs were overall concentration dependent, yet not in a lenear mode. These findings indicate that CND as a free radical scavenger can reduce the βA protein oligomerization once it reaches a critical level in a non-linear mode. The observed CNDs’ properties make it feasible as a potential daignostic and therapeutic agent.

Carbon nanodots for suppressing beta-amyloid (βA) oligomerization in Alzheimer's disease

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.