Dhiman Ghosh

Nov 20, 2024 | nature.com | Dhiman Ghosh |Matthias Schneider |Dzmitry Ashkinadze |Harindranath Kadavath |Peter Güntert |Georg Krainer | +4 more

AbstractThe complex kinetics of disease-related amyloid aggregation of proteins such as α-Synuclein (α-Syn) in Parkinson’s disease and Aβ42 in Alzheimer’s disease include primary nucleation, amyloid fibril elongation and secondary nucleation. The latter can be a key accelerator of the aggregation process. It has been demonstrated that the chaperone domain BRICHOS can interfere with the secondary nucleation process of Aβ42.

Aug 28, 2024 | elifesciences.org | Lukas Frey |Dhiman Ghosh |Bilal Qureshi |David Rhyner

eLife assessment This study presents important findings on the different polymorphs of alpha-synuclein filaments that form at various pH's during in vitro assembly reactions with purified recombinant protein. Of particular note is the discovery of two new polymorphs (1M and 5A) that form in PBS buffer at pH 7. The strength of the evidence presented is convincing. The work will be of interest to biochemists and biophysicists working on protein aggregation and amyloids.

Oct 28, 2023 | biorxiv.org | Lukas Frey |Dhiman Ghosh |Bilal Qureshi |David Rhyner

AbstractThe aggregation of the protein α-synuclein is closely associated with several neurodegenerative disorders and as such the structures of the amyloid fibril aggregates have high scientific and medical significance. However, it seems that there are about as many unique atomic-resolution structures of these aggregates as there are publications describing them.