Does polysaccharide glycogen behave as a promoter of amyloid fibril formation at physiologically relevant concentrations?

Soft Matter. 2021 Feb 19;17(6):1628-1641. doi: 10.1039/d0sm01884h.


We investigated the influence of glycogen (GG), phytoglycogen (PG), mannan (MAN) and cinnamoyl-modified GG (GG-CIN) on amyloid fibril formation. We used hen egg-white lysozyme (HEWL) as a model system and amyloid beta peptide (1-42) (Aβ1-42) as an Alzheimer's disease-relevant system. For brief detection of fibrils was used thioflavin T (ThT) fluorescence assay and the results were confirmed by transmission electron microscopy (TEM). We also deal with the interaction of polysaccharides and HEWL with isothermal titration calorimetry (ITC) and dynamic light scattering (DLS). We found that all polysaccharides accelerated the formation of amyloid fibrils from both HEWL and Aβ1-42. At high but physiologically relevant concentrations of GG, amyloid fibril formation was extremely accelerated for HEWL. Therefore, on the basis of the herein presented in vitro data, we hypothesize, that dietary d-glucose intake may influence amyloid fibril formation not only by influencing regulatory pathways, but also by direct glycogen-amyloid precursor protein molecular interaction, as glycogen levels in tissues are highly dependent on d-glucose intake.

MeSH terms

  • Amyloid beta-Peptides*
  • Amyloid*
  • Dynamic Light Scattering
  • Glycogen
  • Microscopy, Electron, Transmission


  • Amyloid
  • Amyloid beta-Peptides
  • Glycogen