New structurally flexible 1-methyl- and 1,2-dimethyl-imidazolium phosphate ionic liquids (ILs) bearing oligoethers have been synthesized and thoroughly characterized. These novel ILs revealed high thermal stabilities, low glass transitions, high conductivity...

Ion transport measures and details as well as physico-chemical and electrochemical properties are presented for a small set of structurally flexible pyrrolidinium (Pyrr) and morpholinium (Morph) cation-based ionic liquids (ILs),...

Oligomeric and protofibrillar aggregates formed by the amyloid-b peptide (Ab) are believed to be involved in the pathology of Alzheimers disease. Central to Alzheimer pathology is also the fact that the longer Ab 42 peptide is more prone to aggregation than the more prevalent Ab 40 . Detailed structural studies of Ab oligomers and protofibrils have been impeded by aggregate heterogeneity and instability. We previously engineered a variant of Ab that forms stable protofibrils and here we use solid-state NMR spectroscopy and molecular modeling to derive a structural model of these. NMR data are consistent with packing of residues 16 to 42 of Ab protomers into hexameric barrel-like oligomers within the protofibril. The core of the oligomers consists of all residues of the central and C-terminal hydrophobic regions of Ab, and hairpin loops extend from the core. The model accounts for why Ab 42 forms oligomers and protofibrils more easily than Ab 40 .

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