Located in the presynaptic terminals in neurons, the α-synuclein protein is a toxic, aggregating protein playing a major role in Parkinson’s disease. Along with a number of self-assembling proteins involved in various neurodegenerative diseases, α-synuclein undergoes N-acetylglucosamine (GlcNAc) modification post-translationally. The modification occurs on Ser/Thr residues of thousands of proteins, altering their structure and function. Modification of α-synuclein with as little as one single O-GlcNAc unit has been shown to inhibit the proteins aggregation and alter its pathogenic processing.1 Available treatments for Parkinson’s disease merely control the symptoms, there currently exists no therapy that can prevent progression of the disease. The majority of small molecules reported to bind α-synuclein also bind nonselectively to a variety of biomolecules. As such, they are burdened with a potential for inflicting numerous sideeffects. Increasing a leads selectivity via structural optimisation is complicated by the nature of the aggregation process, characterised by unstable intermediate structural conformations and complexes arising throughout. Peptide-based strategies offer biologically active compounds that boast high selectivity due to their ability to establish multiple points of contact with their target.2 Their strong, reversible binding also qualifies peptides as model ex vivo imaging agents. Here we have designed, synthesised and are in the process of evaluating a series of novel bimodal glycopeptides derived from the native α-synuclein sequence for their ability to inhibit pathological αsynuclein aggregation.