Roland Riek is Full Professor of Physical Chemistry at ETH Zurich and Adjunct Professor at the Salk Institute for Biological Studies, La Jolla, California since May 2007. He was born in Bern in 1969, studied Physics at ETH Zurich and remained at ETH to do his PhD with Prof. Kurt Wüthrich at the Institute for Molecular Biology and Biophysics and defended his thesis entitled: ‘NMR structure of the Mouse Prion Protein in 1998. After a few years as postdoc at the Institute for Molecular Biology and Biophysics at ETH, he joined the structural biology laboratory of the Salk Institute for Biological Studies in La Jolla, California in 2001 as assistant professor, in 2006 as associate professor and director of the NMR facility.
The Riek group has contributed in method developments of studying large proteins and in the measurement of very accurate distance restraints that enables the calculation of the structures of ensemble of states giving insights into protein dynamics at atomic resolution including the elucidation of concerted motion. Studying of Membrane Protein Structures and Dynamics The Riek group has structurally and dynamically characterized several membrane proteins and membrane protein complexes including the potassium channel KcsA and the discoidal high density lipoprotein particles (HDL) known as the “good” cholesterol. The high resolution studies allowed insight into the activity of the proteins. Studying protein aggregation from a structural perspective
The Riek group in collaboration with B. Meier (at the ETH) determined several 3D solid state NMR structures of protein aggregates including the published HET-s prion beta-solenoid associated being an infectious structure and a disease-relevant polymorph of Abeta(1-42) amyloids associated with Alzheimer’s disease. In addition, the Riek group contributed significantly in the establishment and study of functional amyloids including the elucidation of the structure-activity relationship of the prion-based immune system of HET-s being functionally and structurally conserved with mammalian necroptosis, and the elucidation of functional mammalian amyloids including hormone storage in secretory granules (including b-endorphins, prolactin, etc.) and the storage of the toxic major basic protein in white blood cells. In parallel, the Riek group showed that the amyloid fold may have been involved in the origin of life quest by demonstrating that amyloid can be enzymatically active and that under prebiotic conditions amyloid may have formed. Within the area of Parkinson’s disease, the Riek group studied a structure-toxicity relationship based on structural work on alpha-Synuclein and the aggregation kinetics at the water air interface.
On the amyloid world hypothesis The Riek group contributed with experimental data on the hypothesis that peptide amyloids may have played a role in the origin of life by demonstrating the self replication of peptide amyloids, the synthesis of peptide amyloids in a prebiotic enviornment, and a symbiotic interplay between membranes and amyloids.
- Riguet, N., Mahul-Mellier, AL., Maharjan, N. et al (2021).. Nuclear and cytoplasmic huntingtin inclusions exhibit distinct biochemical composition, interactome and ultrastructural properties. Nat Commun 12, 6579, Link to the publication.
- Lashuel, H. A. (2021). Rethinking protein aggregation and drug discovery in neurodegenerative diseases. Current Opinion in Chemical Biology 64: 67-75, Link to the publication.
- Mahul-Mellier, A.-L., Burtscher, J., Maharjan, N., Weerens, L., Croisier, M., Kuttler, F., Leleu, M., Knott, G. W., & Lashuel, H. A. (2020). The process of Lewy Body Formation, rather than simply α-synuclein fibrillization, is one of the major drivers of neurodegeneration. Proceedings of the National Academy of Sciences, 117(9), 4971–4982, Link to the publication.