Mechanisms of early amyloid formation and the confining influence of macromolecular crowding (B12)

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This project aims to gain a more detailed understanding of the early prefibrillar growth process of amyloidic aggregates and the influence of a constraining environment. In order to reveal the initial pathways of aggregation and disassembly, size distributions of small transient aggregates (named oligomers) are experimentally studied along the time course of fibrillation. Having started with investigations of disease relevant amyloid peptides in the last funding period, we plan to compare the obtained results to the functional amyloid PTH in the next funding period. In addition, macromolecular crowding will be used to reveal the impact of an outer confinement and to discuss the importance of intermolecular interactions in order to test current models of nucleation and growth.