Our new preprint about alpha-synuclein aggregation in aCSF with Cryo-EM structure. https://doi.org/10.1101/2025.02.21.639308
#Cryo-EM #Alpha-synuclein #VilniusUniversity #science
We study effects of various factors on aggregation kinetics, thermodynamic stability, and structural properties of amyloid-like fibrils and liquid-liquid phase separation phenomena. We believe only comprehensive knowledge of all factors may give a genuine understanding of mechanisms of amyloid self-replication and thus proteinaceous infectivity. We are located at the Life Sciences Center, Vilnius University
Our new preprint about alpha-synuclein aggregation in aCSF with Cryo-EM structure. https://doi.org/10.1101/2025.02.21.639308
#Cryo-EM #Alpha-synuclein #VilniusUniversity #science
Please check out our new publication, "Diverse effects of fluorescent labels on alpha-synuclein condensate formation during liquid-liquid phase separation," via the link below. A great job by Mantas Žiaunys!
This research was funded by the Research Council of Lithuania grant number S-MIP-24-52.
We are also pleased to share two articles from our successful collaborations with scientists from Latvia, Sweden, and Italy:
1. Pro-inflammatory protein S100A9 targeted by a natural molecule to prevent neurodegeneration onset (
https://authors.elsevier.com/c/1jTo0WFfgx3rd )
2. Solid-state NMR backbone chemical shift assignments of α-synuclein amyloid fibrils at fast MAS regime (https://link.springer.com/article/10.1007/s12104-024-10186-2)
Check out our new articles:
1. S100A9 inhibits and redirects prion protein 89-230 fragment amyloid aggregation (https://authors.elsevier.com/c/1jOWAw0NWLCh)
2. Liquid–liquid phase separation of alpha-synuclein increases the structural variability of fibrils formed during amyloid aggregation (https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.17244)
Check out our new preprint titled "Diverse effects of fluorescent labels on alpha-synuclein condensate formation during liquid-liquid phase separation"
A new paper from our sector titled "Formation of Calprotectin Inhibits Amyloid Aggregation of S100A8 and S100A9 Proteins" has been published.
Hello Mastodon,
Our first post is about Liquid-liquid phase separation (LLPS) phenomena, during which proteins form liquid droplets, followed by amyloid aggregation. LLPS is observed in neurodegenerative disorders, cancers and certain cases is related to protein functions in the cell nucleus. Watch below as alpha-synuclein, a protein linked to Parkinson's disease, undergoes LLPS.