Amyloid proteins chaperone effect

However, when the proteins fall on tiie 2D surface of the membrane, tiiis distance is significantly decreased. The effect is potentiated by tiie fact that the attachment of the amyloid protein on the membrane is not stochastic. Indeed, a common feature of amyloid proteins is that they have a marked preference for glycosphingolipids (e.g., gangliosides) that are concentrated in relatively small microdomains of tiie plasma membrane (lipid rafts). Thus, landing on a lipid raft will result in an important concentration of the amyloid protein, and this effect is potentiated by the reduction of dimensionality (Fig. 8.5). Moreover, the head groups of glycolipid clusters will exert a chaperone effect that forces the amyloid protein to adopt a secondary structure, which, depending on the protein-lipid stoichiome, can be either an a-helix or a (3-rich stmcture. ... 

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