Amyloid protein at the membrane surface

Amyloid protein at the membrane surface refers to the pathological interaction between misfolded amyloidogenic proteins—such as amyloid-beta (Aβ), alpha-synuclein (α-syn), and islet amyloid polypeptide (IAPP)—and the lipid bilayer of cell membranes [4, 6]. This interaction is a critical step in the pathogenesis of various neurodegenerative and metabolic diseases, as the membrane surface acts as a catalyst for the misfolding and aggregation of these proteins into toxic oligomers [1, 5]. These oligomeric species can disrupt membrane integrity by forming pores or causing lipid extraction, leading to uncontrolled ion influx, oxidative stress, and eventual cell death [3, 6]. Therapeutic strategies targeting this site aim to displace these toxic species from the membrane or prevent their initial binding, thereby protecting the cell from amyloid-mediated damage [4, 7]. Drugs like squalamine and trodusquemine are currently being investigated for their ability to outcompete amyloid oligomers for membrane binding sites, offering a novel approach to treating conditions like Parkinson's and Alzheimer's diseases [5, 6].

Other names

Membrane-bound amyloid oligomersAmyloid-membrane interfaceMembrane-associated amyloidAmyloid-lipid interactionMembrane-bound alpha-synuclein

Displacement of toxic amyloid oligomers from the cell membrane and inhibition of lipid-induced nucleation.