Abstract: Misfolding and subsequent aberrant self-assembly of certain proteins into toxic amyloid deposits are hallmarks of various diseases, most notably neurodegenerative disorders such as Alzheimer’s disease (AD) and Parkinson’s disease (Chiti and Dobson, 2017). Aromatic residues in amyloidogenic proteins have been shown to be key factors in protein oligomerization and fibrilization, mostly driven by π-π interactions. Together with aromaticity, post-translational modifications can greatly affect a protein’s solubility and conformation and, as a consequence, its propensity to aggregate. Among post-translational modifications, this perspective focuses on protein glycosylation, the decoration of a protein with carbohydrate motifs, its effect on amyloid formation and its employment in the inhibition of protein aggregation.