News

LMNN

The amyloid-beta peptide accumulates to amyloid fibrils that build up dense amyloid plaques. Credit: selvanegra (iStock photos)

Gold nanoparticles uncover amyloid fibrils

— EPFL scientists have developed powerful tools to unmask the diversity of amyloid fibrils, which are associated with Alzheimer’s disease and other neurodegenerative disorders. The scientists made the breakthrough by developing gold nanoparticles that combine with cryogenic transmission electron microscopy, to provide rapid and unprecedented images of fibrils.

The amyloid-beta peptide accumulates to amyloid fibrils that build up dense amyloid plaques. Credit: selvanegra (iStock photos)

Gold nanoparticles uncover amyloid fibrils

— EPFL scientists have developed powerful tools to unmask the diversity of amyloid fibrils, which are associated with Alzheimer’s disease and other neurodegenerative disorders. The scientists made the breakthrough by developing gold nanoparticles that combine with cryogenic transmission electron microscopy, to provide rapid and unprecedented images of fibrils.

© 2020 EPFL

New insights into the processes that cause Parkinson's disease

— In a breakthrough for Parkinson’s disease, scientists at EPFL have reconstructed the process by which Lewy bodies form in the brain of patients. The study offers new insights into how Parkinson’s disease begins and evolves, and opens up a set of potential new treatment targets.

Hilal Lashuel. Credit: EPFL - Alain Herzog

EPFL and AbbVie collaborate to advance Alzheimer's research

— EPFL and AbbVie, a global biopharmaceutical company, have entered into a three-year collaboration agreement to advance research in and development of novel mechanism-based therapeutic strategies for Alzheimer’s disease.

Neurofibrillary tangles (dark purple, elongated structure) in the hippocampus of an old person with Alzheimer-related pathology (credit: Wikimedia Commons user Patho)

Alzheimer's: Breaking the “code of Tau”

— Tau protein is one of the major targets in Alzheimer’s disease. EPFL scientists have now found a way to crack the previously inaccessible set of changes that turn Tau into a toxic molecule, known as the “code of Tau”.

A cell visualized with the PRISM method © T. Lasser/EPFL

Super-resolution microscopy in both space and time

— In a breakthrough for biological imaging, EPFL scientists have developed the first microscope platform that can perform super-resolution spatial and temporal imaging, capturing unprecedented views inside living cells. The landmark paper is published in Nature Photonics.

Neurofibrillary tangles (credit: Jose Luis Calvo Martin & Jose Enrique Garcia-mauriño Muzquiz/iStock)

Alzheimer's Tau protein forms toxic complexes with cell membranes

— Alzheimer’s disease is caused by tangles in the brain made up of malfunctioning aggregated Tau proteins. Scientists at EPFL have discovered a new toxic form of Tau that forms as a result of its interaction with cell membranes. The research is published in Nature Communications and provides novel insights into possible mechanisms by which this protein moves in the brain and kills neurons.

The location of the htt gene on chromosome 4 (credit: Genetics Home Reference/NCBI) and the 3D structure of huntingtin (EBI)

Imaging a killer: High-resolution structural analysis of Huntingtin

— An international team of researchers has obtained the first ever atom-level structural insights into bona fide monomeric forms of Httex1, a part of the huntingtin gene that is thought to underlie Huntington’s disease.

The structure of huntingtin (EBI)/iStock photos (human sketch)

Cracking the code of Huntington's disease

— Huntington’s disease is caused by a gene mutation that causes a protein to build up in the brain. In a world first, EPFL scientists have synthesized and studied modified forms of a mutant part of the protein, deepening our understanding of how it contributes to the disease, and pointing to new therapeutic strategies for treating it.

A mouse neuron with Lewy bodies (green) © M. Fares (EPFL)

A better model for Parkinson's

— Scientists at EPFL solve a longstanding problem with modeling Parkinson’s disease in animals. Using newfound insights, they improve both cell and animal models for the disease, which can propel research and drug development.

© 2015 EPFL

Fibril growth and seeding are key to Parkinson's disease

— 08.07.15 – EPFL scientists have discovered how the aggregation process of a protein could lead to Parkinson’s disease. The study opens the way for entirely new treatment strategies.

Credit: ThinkStock

A new tool for understanding Parkinson's disease

— EPFL scientists have developed a new method that can accurately simulate the chemical modification of the protein behind Parkinson’s disease. The technique, has opened a new way of understanding Parkinson’s, and can be expanded to other proteins and diseases as well.

© Suraj Rajan/Wikipedia: A Lewy body...

Parkinson's is not a single disease

— Hilal Lashuel and his group (EPFL Brain Mind Institute) have discovered that some of the gene mutations underlying familial Parkinson’s disease work through multiple ways in the cell. These findings can impact our pharmaceutical strategies for treating all forms of the disease.

Amlyoid beta aggregating outside neurons. (Image: ThinkStock)

Protein elasticity underlies Alzheimer's and Parkinson's disease

— Researchers from EPFL have studied the evolution of amyloid-beta and alpha-synuclein from peptides to fibrillar aggregates, and have mapped out how gradually the fibril’s stiffness increases in the process.

© 2013 EPFL

The many faces of α-synuclein.

— The many faces of α-synuclein: from structure and toxicity to therapeutic target. (Review)

© 2012 EPFL

Discovery of a novel aggregation domain in the Huntingtin protein.

— Discovery of a Novel Aggregation Domain in the Huntingtin Protein: Implications for the Mechanisms of Htt Aggregation and Toxicity.

© par Argonne National Laboratory

Chemical Biology of Parkinson's disease.

— Elucidating the role of C-terminal post-translational modifications using protein semisynthesis strategies: α-synuclein phosphorylation at tyrosine 125.