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. 2012 Mar 21;13(3):3801–3819. doi: 10.3390/ijms13033801

Table 1.

Effect of osmolytes addition to several fibrillating proteins.

Osmolyte Aβ40 Aβ42 α-synuclein polyQ Immunoglobulin light chains Glucagon 1 insulin lysozyme
Glucose oligomerization [24] oligomerization [24] collapse no effect minor effect [14]
Sucrose oligomerization [24] oligomerization [24] no effect no/minor effect [14,44] reduced aggregation [25,45]
Fructose no effect[24] no effect [24] minor effect [14]
Galactose induced fibrillation [24] induced fibrillation [24]
Mannose induced fibrillation [24] induced fibrillation [24]
Sorbitol longer lag, more stable fibrils [46] no effect
Glycerol oligomerization [33] no effect no effect [25]
Trehalose slower/no fibrillation [36,37] oligomerization (toxic) [36] reduced aggregation in mice [47] no effect reduced/slower fibrillation [14,44] increasing B1 [48], reduced aggregation [45]
Gly faster fibrillation [35] faster fibrilation no effect [25]
Pro amorphous aggregates [27] polymorphism inhibits aggregation [25]
Taurine faster fibrillation [35] slower fibrillation
Ectoine longer lag time, more oligomers, lower toxicity[40] faster fibrilation highly reduced fibrillation [44]
Betaine faster fibrillation [27] longer lag, more stable fibrils [46] faster fibrilation highly reduced fibrillation [44] increasing B2 [48]
Sarcosine faster fibrillation, polymorphism Tm of unfolding increases by 22°, but the unfolded lysozyme aggregates [12]
TMAO little effect [37]; oligomerization [33] folded oligomer/enhanced fibrillation [28] amorphous aggregates [27]

Notes:

1

Based on results in this study.

2

B: osmotic second virial coefficient.

An increasing value means more attractive forces between molecules.