Membrane-Protein Interactions Are Key to Understanding Amyloid Formation
"... The authors have managed to navigate a substantial portion of the still-growing literature to summarize the key membrane characteristics that are involved in promoting or suppressing oligomer formation. On the basis of general considerations, it is clear that membrane- mediated aggregation should depend on physical properties, such as net charge per unit area and hydrophobicity and hydrophilicity. Indeed, it has been found that membranes composed of anionic phospholipids (such as phosphatidylserine and phosphatidyglycerol) catalyze the formation of amyloids.9 The mechanical properties of the fluid membranes also affect the interaction between proteins, as demonstrated using continuum theories. Thus, cholesterol (Ch) or crowding agents that affect the overall membrane fluidity also affect aggregation,10 as summarized succinctly in Bucciantini et al.’s Perspective. It is likely that theoretical ideas in the soft matter field could be profitably used to predict generic aspects of membrane-mediated interpeptide interaction. The specific details of membrane composition, which cannot be easily taken into account using only the general physicochemical properties, require a deeper understanding of biological membranes. ... ..."