Protein amyloid fiber formation is the pathological hallmark in various neurodegenerative diseases such as Parkinson’s and Alzheimer’s. The physico-chemical origin of protein fibrilation, as well as the role that hydration-water might play remain elusive. We combine elastic and quasi-elastic neutron spectroscopy and molecular dynamics simulations on the intrinsically disordered proteins α-synuclein (involved in Parkinson disease) and tau (involved in Alzheimer disease) to investigate both structural and dynamical properties of the protein-hydration water system. One of our findings is an increased water translational diffusion on fiber surfaces, suggesting that hydration-water entropy might be one of the driving forces for amyloid fiber formation.
Kevin Pounot
(Institut für Angewandte Physik, Universität Tübingen, 72076 Tübingen, Germany & Institut Max von Laue – Paul Langevin (ILL), CS 20156, F-38042 Grenoble, France)
Giorgio Schiro
(Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale, F-38000 Grenoble, France)
Yann Fichou
(IECB / CBMN / Univ. Bordeaux, France)
Martine Moulin
(Institut Max von Laue – Paul Langevin (ILL), CS 20156, F-38042 Grenoble, France)
Michaela Zamponi
(Forschungszentrum Jülich GmbH, Jülich Centre for Neutron Science at Heinz Maier-Leibnitz Zentrum)
Michael Haertlein
(Institut Max von Laue – Paul Langevin (ILL), CS 20156, F-38042 Grenoble, France)
Tilo Seydel
(Institut Max von Laue – Paul Langevin (ILL), CS 20156, F-38042 Grenoble, France)
Annette Langkilde
(Department of Drug Design and Pharmacology, University of Copenhagen, Universitetsparken 2, 2100 Copenhagen, Denmark)
Douglas J. Tobias
(Department of Chemistry, University of California, Irvine, Irvine, California 92697, United States)
Prof.
Frank Schreiber
(Uni Tübingen, Angewandte Physik)
Martin Weik
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