Blocking amyloid lipid interaction as a therapeutic strategy

Abstract

Protein aggregation is the core feature in all amyloid diseases. The aggregation process results in a heterogeneous mixture of aggregates, ranging from small oligomers to large β- sheet rich fibrils. Due to the commonality of protein aggregation across these diseases, significant effort has been targeted toward developing aggregation altering agents as potential therapeutics, yet no effective treatment has been developed. Many of these amyloids (β-amyloid, α-synuclein, islet amyloid polypeptide, etc.) strongly interact with lipid membranes, leading to membrane damage and dysfunction.