Amyloidogenic peptides aggregated to large molecular assemblies are a hallmark of several diseases including Parkinson\u2019s, Huntington\u2019s, and Alzheimer\u2019s disease as well as type II diabetes. Although each of these diseases gives rise to a very distinctive clinical picture, amyloid fibrils share the cross-\u03b2\u00a0structure as a common structural motif. Within this motif, the peptide strands are linked via lateral \u03b2-sheet-turn-\u03b2-sheet structures that result in fiber-like aggregates with diameters of a few nanometers and lengths up to several micrometers.<\/p>\n
The central question that will be addressed is how electrostatic and hydrophobic interactions compete within the central core region of A\u03b2(1-40) fibrils. By means of extensive molecular dynamics simulations we investigated a series of rationally mutated A\u03b2(1-40) variants, which feature charged side chains in the otherwise hydrophobic central core region of the fibril. Our study suggests considerable structural changes compared to wild type A\u03b2(1-40) fibrils that are consistent with parameters measured in solid-state NMR experiments.<\/p>\n
Location: MLU, Von-Danckelmann-Platz 3, SR 1.09\r\nTime: 3.30pm<\/pre>\n","protected":false},"excerpt":{"rendered":"