Comparison of N-Acetyl-Glucosamine to Other Monosaccharides Reveals Structural Differences for the Inhibition of α-Synuclein Aggregation.

ABSTRACT: O-GlcNAc modification of the microtubule associated protein tau and α-synuclein can directly inhibit the formation of the associated amyloid fibers associated with major classes of neurodegenerative diseases. However, the mechanism(s) by which this posttranslational modification (PTM) inhibit amyloid aggregation are still murky. One hypothesis is that O-GlcNAc simply acts as a polyhydroxylated steric impediment to the formation of amyloid oligomers and fibers. Here, we begin to test this hypothesis by comparing the effects of O-GlcNAc to other similar monosaccharides-glucose, N-acetyl-galactosamine (GalNAc), or mannose-on α-synuclein amyloid formation. Interestingly, we find that this quite reasonable hypothesis is not entirely correct. More specifically, we use

SUBMITTER: Galesic A 

PROVIDER: S-EPMC8142260 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature