PrP (106-128), is a 23-residue peptide fragment. Prion diseases are characterized by the accumulation of conformational modifications of cellular prion proteins into a pathogenic conformation, called scrapie PrPsc, which is the main molecular process involved in the pathogenesis of prion diseases. Amyloid formation is a key pathological feature of prion disease and is considered a major contributing factor to neurodegeneration. We presented a systematic analysis of the impact of phospholipid liposomes of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1’-rac-glycerol) (POPG) in the absence or presence of cholesterol, on the amyloidogenesis of PrP (106-128). Our ThT binding assay and atomic force microscopy (AFM) demonstrate that POPC vesicles do not significantly influence the aggregation kinetics of peptides. In contrast, the anionic lipid vesicles of POPG and POPG/Cholesterol accelerate aggregation in a concentration-dependent manner. We examined the interaction of phospholipids with PrP (106-128) to analyze the effect of membrane composition and charge on peptide conformation and fibril formation. This study supports the notion that the interaction between fragment prions (106-128) and lipid membranes may play a role in PrP transformation and proposes a possible mechanism of interaction based on our results and observations.

Effects of phospholipid liposomes on prion peptide (106-128) amyloidogenesis

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