Sara Linse

Aug 17, 2024 | nature.com | Catherine Xu |Georg Meisl |Ewa Andrzejewska |Georg Krainer |Irina Edu |Michele Vendruscolo | +1 more

AbstractOligomeric species arising during the aggregation of α-synuclein are implicated as a major source of toxicity in Parkinson’s disease, and thus a major potential drug target. However, both their mechanism of formation and role in aggregation are largely unresolved. Here we show that, at physiological pH and in the absence of lipid membranes, α-synuclein aggregates form by secondary nucleation, rather than simple primary nucleation, and that this process is enhanced by agitation.

Feb 7, 2024 | pubs.rsc.org | Natalie Golota |Brian Michael |Edward P. Saliba |Sara Linse

Structural Characterization of E22G Aβ1-42 Fibrils via 1H detected MAS NMR Amyloid fibrils have been implicated in the pathogenesis of several neurodegenerative diseases, the most prevalent example being Alzheimer's disease (AD). Despite the prevalence of AD, relatively little is known about the structure of the associated amyloid fibrils.

Sep 20, 2023 | jbc.org | Rebecca Frankel |Emma Sparr |Sara Linse

AbstractThe double nucleation mechanism of amyloid β (Aβ) peptide aggregation is retained from buffer to cerebrospinal fluid (CSF), but with reduced rate of all microscopic processes. Here we used a bottom-up approach to identify retarding factors in CSF. We investigated the Aβ42 fibril formation as a function of time in the absence and presence of ApoA-I, recombinant high-density lipoprotein (rHDL) particles, or lipid vesicles.

Jun 27, 2023 | nature.com | Daoyuan Qian |Michele Vendruscolo |Sara Linse

Cite this articleMichaels, T.C.T., Qian, D., Šarić, A. et al. Amyloid formation as a protein phase transition. Nat Rev Phys (2023). https://doi.org/10.1038/s42254-023-00598-9Download citationAccepted: 12 May 2023Published: 27 June 2023DOI: https://doi.org/10.1038/s42254-023-00598-9Share this articleAnyone you share the following link with will be able to read this content:Sorry, a shareable link is not currently available for this article.

Jun 6, 2023 | pubs.rsc.org | Sara Linse |Tuomas Knowles

Amyloids and protein aggregation Sara Linse a  and  Tuomas Knowles b   Abstract A general discovery in protein science in the past few decades has been the finding that a number of unrelated proteins and peptides all have a marked propensity to form amyloid fibrils in vivo and in vitro. These structures have become known as the pathological hallmark of some of the most prevalent neurodegenerative diseases.