The protein alpha-synuclein aggregates are constituents of Lewy bodies, a histological hallmark of the synuceinopathies Parkinson's disease, Lewy body dementia and multiple system atrophy.
Elucidating the forms alpha-synuclein molecules adopt upon staking within aggregates is key for the design of ligands targeting those aggregates. Such ligands could attach along or at the ends of the resulting fibrils and affect their surface properties or their ability to elongate and thus limit the pathological processes involved in synucleinopathies.
Partner CNRS within a collaborative study with experts in Cryo-Electron microscopy recently determined a new structure for alpha-synuclein fibrils, down to an atomic level. Those fibrils, when injected into rodent models, cause the development of symptoms characteristic of Parkinson's disease.Read more
Cryo-EM of two polymorphic structures of alpha-synuclein fibrils by Luc Bousset and Ronald Melki from CNRS has just be published on eLife:. Read the publication.
As part of the LMB-365 project, Michel Goedert was recognised this week for 35 years at LMB (The Medical Research Council Laboratory of Molecular Biology) focussing on the study of Alzheimer’s disease, helping to show that the aggregation of tau protein is sufficient to cause neurodegeneration and dementia. LMB 365 – Day 336.
This project receives funding from the Innovative Medicines Initiative 2 Joint Undertaking (www.imi.europa.eu) under grant agreement No 116060. This Joint Undertaking receives support from the European Union’s Horizon 2020 research and innovation programme and EFPIA.
This work is supported by the Swiss State Secretariat for Education‚ Research and Innovation (SERI) under contract number 17.00038.
The opinions expressed and arguments employed herein do not necessarily reflect the official views of these funding bodies.