1 iNano-School, Science and Technology, Aarhus University2 Interdisciplinary Nanoscience Center, Science and Technology, Aarhus University3 Department of Molecular Biology, Faculty of Science, Aarhus University, Aarhus University4 Interdisciplinary Nanoscience Center - INANO-MBG, iNANO-huset, Interdisciplinary Nanoscience Center, Science and Technology, Aarhus University5 Interdisciplinary Nanoscience Center - INANO-MBG, iNANO-huset, Interdisciplinary Nanoscience Center, Science and Technology, Aarhus University
Over the last few decades, protein aggregation gone from being an irritating side product in the test tube to becoming a subject of great interest. This has been stimulated by the realization that a large and growing number of diseases is associated with the formation and accumulation of proteins aggregates 1. The ability to form amyloid structures has also been exploited by living systems, where proteins forming fibrils during the normal life-cycle have functional rather than disease associated properties 2; 3; 4; 5. Thus, understanding the structural features of fibrils, as well as the processes leading to their formation is important for designing new drugs as well as in development of new nano-biomaterials such as nano-tubes, wires, scaffolds etc. 6. Understanding the process of amyloid formation requires an ability to reproduce this aggregation under controlled circumstances, in other words the development of robust aggregation assays. The following review focuses on ways in which this has been developed for α-synuclein (αSN), a key player in the development of Parkinson’s Disease. We focus specifically on the formation of the amyloid end product, rather than ways to optimize accumulation of the presumably cytotoxic prefibrillar aggregate, whose properties are deserving of a separate chapter.