Various synaptosomal and liposomal studies have suggested that GM1 accelerates formation of amyloid fibrils (Yamamoto et al., 2004; Zha et al., 2004) . Further analysis of the role of lipid rafts in Aβ aggregation have confirmed that raft proteins do not play a significant role in this process as proteinase K or SDS treatment did not affect the aggregation-promoting capacity of the rafts. Moreover, the cholesterol-depleting agent methyl-βcyclodextrin (MβCD) also did not have an effect on Aβ oligomerization (Kim et al., 2006) . Further cell studies reinforce the role of gangliosides in Aβ aggregation. Rafts taken from ganglioside rich cells (C 2 C 12 ) were able to induce Aβ aggregation more potently than ganglioside-poor cells (HeLa and SK-N-MC). Similarly, rafts isolated from brain tissue rich in gangliosides were able to increase Aβ aggregation compared to rafts isolated from the liver with lower ganglioside content. Also, CHO-K1 cells genetically deficient in the synthesis of complex gangliosides had lower levels of Aβ aggregation than the wild type cells (Kim et al., 2006) .