The modification of intracellular proteins by the monosaccharide <i>N</i>-acetyl-glucosamine (O-GlcNAc) is indispensable for life in mammals and contributes to a variety of human diseases. Neurodegenerative diseases are typically associated with the formation of toxic protein aggregates. Notably several of these proteins are O-GlcNAcylated. Previous data have demonstrated that O-GlcNAcylation of the protein tau inhibits its aggregation; however, was yet known about other aggregation-prone proteins. To begin to address this knowledge gap, I will present the use of protein semi-synthesis to first prepare site-specifically O-GlcNAcylated α-synuclein, the major aggregating protein in Parkinson’s disease, and then characterize the consequences of O-GlcNAc on its aggregation and cellular toxicity.

Site-specific investigation of O-GlcNAc modifications using synthetic proteins

251st National Meeting (2016)

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