“…A growing body of evidence indicates that lipids can uniquely alter the aggregation rates of amyloidogenic proteins. ,,,− For instance, Matveyenka and co-workers demonstrated that zwitterionic phosphatidylcholine (PC) could strongly inhibit insulin and lysozyme aggregation. ,, At the same time, anionic lipids, such as phosphatidylserine (PS) and cardiolipin (CL), on the contrary, accelerated the aggregation of both proteins. , It was also found that lipids not only altered the rates of protein aggregation but also uniquely modified the secondary structure of amyloid oligomers and fibrils formed in their presence. ,,, Such aggregates exerted drastically different cell toxicity compared to that of the oligomers and fibrils formed in the lipid-free environment. , For instance, insulin oligomers formed in the presence of PC were found to be significantly less toxic than protein oligomers formed in the presence of PS and CL. , However, amyloid fibrils formed by amyloid β 1–42 in the presence of CL and cholesterol (Cho) exhibited much greater cell toxicity compared to that of amyloid β 1–42 fibrils formed in the lipid-free environment . The results recently reported by Jakubec and co-workers showed that Cho strongly accelerated aggregation of α-synuclein (α-syn), a small protein that is linked to the onset and progression of Parkinson’s disease . This and other pieces of experimental evidence suggest that Cho can be an important player in the aggregation of amyloidogenic proteins .…”