Skip to main content

and
  1. Article

    Open Access

    Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils

    Many proteins self-assemble to form amyloid fibrils, which are highly organized structures stabilized by a characteristic cross-β network of hydrogen bonds. This process underlies a variety of human diseases a...

    Alyssa Miller, Sean Chia, Ewa Klimont, Tuomas P. J. Knowles in Communications Biology (2024)

  2. Article

    Open Access

    The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends

    Molecular chaperones contribute to the maintenance of cellular protein homoeostasis through assisting de novo protein folding and preventing amyloid formation. Chaperones of the Hsp70 family can further disagg...

    Matthias M. Schneider, Saurabh Gautam, Therese W. Herling in Nature Communications (2021)

  3. Article

    Open Access

    Controlled self-assembly of plant proteins into high-performance multifunctional nanostructured films

    The abundance of plant-derived proteins, as well as their biodegradability and low environmental impact make them attractive polymeric feedstocks for next-generation functional materials to replace current pet...

    Ayaka Kamada, Marc Rodriguez-Garcia, Francesco Simone Ruggeri in Nature Communications (2021)

  4. Article

    Open Access

    Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers

    Significant efforts have been devoted in the last twenty years to develo** compounds that can interfere with the aggregation pathways of proteins related to misfolding disorders, including Alzheimer’s and Pa...

    Francesco Simone Ruggeri, Johnny Habchi, Sean Chia in Nature Communications (2021)

  5. No Access

    Article

    Biomolecular condensates undergo a generic shear-mediated liquid-to-solid transition

    Membrane-less organelles resulting from liquid–liquid phase separation of biopolymers into intracellular condensates control essential biological functions, including messenger RNA processing, cell signalling ...

    Yi Shen, Francesco Simone Ruggeri, Daniele Vigolo, Ayaka Kamada in Nature Nanotechnology (2020)

  6. Article

    Open Access

    Single molecule secondary structure determination of proteins through infrared absorption nanospectroscopy

    The chemical and structural properties of biomolecules determine their interactions, and thus their functions, in a wide variety of biochemical processes. Innovative imaging methods have been developed to char...

    Francesco Simone Ruggeri, Benedetta Mannini, Roman Schmid in Nature Communications (2020)

  7. Article

    Open Access

    Microfluidic deposition for resolving single-molecule protein architecture and heterogeneity

    Scanning probe microscopy provides a unique window into the morphology, mechanics, and structure of proteins and their complexes on the nanoscale. Such measurements require, however, deposition of samples onto...

    Francesco Simone Ruggeri, Jerome Charmet, Tadas Kartanas in Nature Communications (2018)

  8. No Access

    Article

    Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes

    Alzheimer’s disease is a neurodegenerative disorder associated with the aberrant aggregation of the amyloid-β peptide. Although increasing evidence implicates cholesterol in the pathogenesis of Alzheimer’s diseas...

    Johnny Habchi, Sean Chia, Céline Galvagnion, Thomas C. T. Michaels in Nature Chemistry (2018)