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Brain accumulation and aggregation of amyloid- (A) peptides is a critical step in the pathogenesis of Alzheimer's disease (AD). Full-length A peptides (mainly A1-40 and A1-42) are produced through sequential proteolytic cleavage of the amyloid precursor pr ...

SPRINGER2019

Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

Henning Paul-Julius Stahlberg, Ricardo Cesar Guerrero Ferreira, Pratibha Kumari

Intracellular inclusions rich in alpha-synuclein are a hallmark of several neuropathological diseases including Parkinson’s disease (PD). Previously, we reported the structure of alpha-synuclein fibrils (residues 1–121), composed of two protofibrils that a ...

2019

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The far-UV spectral window widely used for the conformational analysis of biomolecules is not easily covered with broad-band lasers. This has made it difficult to use circular dichroism (CD) spectroscopy to directly follow fast structure changes. By combin ...

AMER CHEMICAL SOC2019

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The present invention is directed to a method of treating an amyloid-3 peptide disease in a subject in need thereof, the method comprising administering to the subject a therapeutically effective amount of a compound that enhances mitochondrial proteostasi ...

2018

Calpain-mediated tau fragmentation is altered in Alzheimer's disease progression

Andrea Pfeifer, Andreas Muhs

The aggregation of intracellular tau protein is a major hallmark of Alzheimer's disease (AD). The extent and the stereotypical spread of tau pathology in the AD brain are correlated with cognitive decline during disease progression. Here we present an in-d ...

NATURE PUBLISHING GROUP2018

Enhancing mitochondrial proteostasis reduces amyloid-beta proteotoxicity

Johan Auwerx, Davide D'Amico, Adrian Schmid, Norman Lionel Moullan, Vincenzo Sorrentino, Hongbo Zhang, Francesca Potenza, Solene Rietsch

Alzheimer's disease is a common and devastating disease characterized by aggregation of the amyloid-beta peptide. However, we know relatively little about the underlying molecular mechanisms or how to treat patients with Alzheimer's disease. Here we provid ...

Nature Publishing Group2017

Amyloid Fibril Polymorphism: Almost Identical on the Atomic Level, Mesoscopically Very Different

Henning Paul-Julius Stahlberg

Amyloid polymorphism of twisted and straight beta-endorphin fibrils was studied by negative-stain transmission electron microscopy, scanning transmission electron microscopy, and solid-state nuclear magnetic resonance spectroscopy. Whereas fibrils assemble ...

American Chemical Society (ACS)2017

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Cells are extremely complex systems able to modify actively their metabolism and behaviour in response to environmental conditions and stimuli, such as pathogenic agents or drugs. The comprehension of these responses is central to understand the molecular ...

Springer Nature2017

Nanoplasmonic mid-infrared biosensor for in vitro protein secondary structure detection

Giovanni Dietler, Hilal Lashuel, Hatice Altug, Francesco Simone Ruggeri, Dordaneh Etezadi, John Blaine Warner IV

Plasmonic nanoantennas offer new applications in mid-infrared (mid-IR) absorption spectroscopy with ultrasensitive detection of structural signatures of biomolecules, such as proteins, due to their strong resonant near-fields. The amide I fingerprint of a ...

Springer Nature2017

The role of the polyglutamine and N-terminal domains in regulating the aggregation and structural properties of Huntingtin Exon 1

Sophie Vieweg

Huntington Disease (HD) is caused by a CAG repeat expansion in the huntingtin gene leading to the formation of mutant Huntingtin protein (Htt) with an expanded polyglutamine (polyQ) domain (>36Q). Generation of short N-terminal Htt fragments by proteolysis ...

EPFL2017