The link of gangliosides with AD pathology has been mostly related to their localization in lipid rafts which have been suggested to act as a platform for GM1-induced aggregation of Aβ peptide (Parton, 1994; Zha et al., 2004; Ariga et al., 2008) . Labeled Aβ shows high affinity for GM1 containing membranes, suggesting that GM1 acts as an Aβ binding molecule (Kakio et al., 2004) . It has been suggested that the N-terminal region of Aβ interacts with GM1 clusters through hydrogen bonding and electrostatic interactions (Lemkul and Bevan, 2011) . It was also suggested that cholesterol may facilitate GM1 clustering (Kakio et al., 2001) . Extraction of cortical lipid rafts from human AD brains showed an increase in both GM1 and GM2 (Molander-Melin et al., 2005) despite an overall reduction of gangliosides (Ariga et al., 2008) . There are data indicating that gangliosides accumulate in senile plaques and that they may be involved in the conversion of Aβ to a neurotoxic oligomeric form (Molander-Melin et al., 2005; Okada et al., 2008) .