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].
References
[1] J. Greenwald, M. Friedmann, Roland Riek, Angewandte Chemie 53, 11609 (2016). (link)
[2] M. Wälti, F. Ravottie, H. Aral, C. Glabe, J. Wall, A. Bockmann, PO. Guntert, B. Meier, R. Riek, PNAS 113, E4976 (2008). (link)
[3] R. Riek and D. Eisenberg, Nature 539, 227 (2016) (link)