The process of aggregation and subsequent deposition of the peptide amyloid-β (Aβ) on neuronal membranes, which causes disruption of the normal neuronal functions, is generally accepted to be one of the fundamental causes of Alzheimer’s disease (AD). The factors responsible for Aβ aggregation and the mechanism of aggregation are not yet fully understood. Among other factors, ganglioside GM1 is believed to act as a modulator which promotes the aggregation of Aβ. However, the role of the individual saccharides of GM1 ganglioside in Aβ aggregation is not known. In the current research, acrylamide based glycomonomers with either glucose or galactose pendant groups were synthesized, maintaining the stereochemistry of the saccharides in GM1. The monomers were characterized via <sup>1</sup>H-NMR and ESI. Stereospecific glycopolymers were synthesized in solution via aqueous reversible addition-fragmentation chain transfer polymerization (RAFT) and glycopolymer brushes were synthesized on the surfaces of silicon wafers via UV-initiated free radical polymerization. Glycopolymers synthesized in solution and on surfaces will be utilized as models to mimic Aβ/GM1 saccharide interactions in the neuronal membranes.

Synthesis of stereospecific glycopolymers as models to mimic amyloid-β peptide/saccharide interactions

251st National Meeting (2016)

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