Roland Riek1, Marielle Wälti1, Cedric Eichmann, and Jason Greenwald1
1Vladimir Prelog Weg 2, ETH, ETH Hönggerberg, CH-8093 Zurich
Protein aggregation is observed in many diseases including Alzheimer’s disease. These protein aggregates are termed amyloids. Amyloids are composed of pairs of tightly interacting, many-stranded, repetitive, inter-molecular beta-sheets termed the cross-beta-sheet structure. Because of this structure, amyloids can grow by recruitment of the same protein while their repeat can transform a weak activity into a potent one through cooperativity and avidity. Thus, an amyloid has the potential to replicate itself, and can be adaptive to its environment, yielding eventually cell-to-cell transmissibility, prion infectivity, and toxicity. Here, we discuss these structure-based properties within the context of Alzheimer’s disease and Parkinson’s disease from a structural perspective. In addition, we discuss a potential role of amyloids in the origin of life [1-3].
 J. Greenwald, M. Friedmann, Roland Riek, Angewandte Chemie 53, 11609 (2016). (link)
 M. Wälti, F. Ravottie, H. Aral, C. Glabe, J. Wall, A. Bockmann, PO. Guntert, B. Meier, R. Riek, PNAS 113, E4976 (2008). (link)
 R. Riek and D. Eisenberg, Nature 539, 227 (2016) (link)