| Website | http://www.amyloid.bti.vu.lt/ |
| Place | VIlnius University |
Exciting news — our latest publication on the 14-3-3 protein family is out!
In this study, we systematically characterised all members of the 14-3-3 family for two key biophysical properties: amyloid fibril formation and liquid-liquid phase separation (LLPS) — shedding new light on the structural versatility of these important regulatory proteins.
New preprint from our sector about 14-3-3 family amyloid aggregation and liquid-liquid phase separation
https://www.biorxiv.org/content/10.64898/2026.01.07.698245v1
Our new publication is about alpha-synuclein fibrils formed in artificial cerebrospinal fluid.
advanced.onlinelibrary.wiley.com/doi/10.1002/...
Two new articles from our lab:
Calcium-Dependent S100A8 Amyloid Fibril Formation via S100A1-Mediated Transient Interaction https://pubs.acs.org/doi/10.1021/acschemneuro.5c00086
Heterotypic Droplet Formation by Pro-Inflammatory S100A9 and Neurodegenerative Disease-Related α-Synuclein https://pubs.acs.org/doi/10.1021/acs.biomac.5c00130
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
α-Synuclein (aSyn) is an intrinsically disordered protein involved in neurotransmission and synaptic plasticity. The pathological aggregation of this protein is a hallmark of synucleinopathies such as Parkinson’s disease (PD) or Multiple System Atrophy (MSA). Misfolded aSyn, which primarily originates in cell cytosol, transmits between neurons, promoting a prion-like propagation. However, the extracellular environments such as interstitial and cerebrospinal fluids (ISF & CSF) play a major role in its clearance and pathological transformation. The molecular components of CSF, including proteins, glycosaminoglycans, and metal ions may influence the aggregate morphology, structure and cytotoxicity to cells. To better understand how extracellular composition affects aggregates and their formation, we employed artificial cerebrospinal fluid (aCSF) to mimic potential aggregation processes occurring in CSF. We observed distinct aCSF-specific aSyn fibrils that exhibited low stability outside aCSF, and the removal of key CSF components led to its structural alterations. Cryo-electron microscopy revealed that these fibrils possess an electron density pocket coordinated with polar basic AAs (K43, K45, H50) that is also observed in aggregates obtained from MSA patients. Our findings illustrate the importance of physiologically relevant conditions in studying aSyn aggregation and may explain why disease-related fibril structure replication in vitro has not yet been successful. ### Competing Interest Statement The authors have declared no competing interest.
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.