“…These include: (i) the self-assembly and deposition of multiple types of fibrillar and globular structures and polymorphic assemblies both in solution and on membrane surfaces; and (ii) the formation of heterogeneous ionic pores spanning the lipid bilayer that is linked to the pathogenicity of these molecules. These later findings are supported by multiple independent reports regarding the capability of Aβ42 peptides [2 hydrophobic amino acid residues (isoleucine and alanine) longer (at the C-terminal) than Aβ40] to form up to 2.4-nm diameter pores through lipid bilayer membranes (Lashuel et al, 2002; Connelly et al, 2012; Sciacca et al, 2012; Ullah et al, 2015; Di Scala et al, 2016; Jang et al, 2016; Davidson, 2019; Hicks et al, 2019; Nguyen et al, 2019; Sun et al, 2019; Österlund et al, 2019). Interestingly, the slightly longer and more hydrophobic Aβ42-based peptide assemblies in oligomeric preparations have been observed to form voltage-independent, non-selective ion channels in contrast to Aβ40 peptide-based oligomers, fibers, and monomers which do not generally support pore structure formation (Bode et al, 2017, 2019; Nguyen et al, 2019).…”