Alzheimer’s and Parkinson’s disease are the most common neurodegenerative disorders. These diseases are characterized by aggregation of tau and alpha synuclein proteins. Neuroscientists created many disease models to study these incurable disorders, each having strengths and weaknesses^1,2.

One model uses active preformed fibrils to induce protein aggregation in vivo or in vitro. Preformed fibrils can seed in cell culture or animal models to cause normal protein monomers to aggregate, leading to disease progression³. StressMarq is currently the only manufacturer of alpha synuclein and tau pre-formed fibrils for neurodegenerative disease research.

The Michael J. Fox Foundation emphasizes the need to sonicate alpha synuclein pre-formed fibrils before performing experiments¹. In this video, we explain why we recommend the sonication of our pre-formed fibrils prior to use. Watch here to learn why sonication of our fibril constructs produce the most effective seeding pathology in neurodegenerative research.

The Effect of Sonication on Preformed Fibrils

Read our blog post for details about how sonication affects alpha synuclein preformed fibrils.

Fibril Size

Sonication shortens the length of alpha synuclein pre-formed fibrils. It has been previously shown that alpha synuclein fibrils of 50nm or less demonstrate more effective seeding capability, leading to more efficent protein aggregation³.

Fibril Solubility

Sonication increases alpha synuclein fibril solubility. Having solubilized fibrils in solution prior to experimentation is associated with increased seeding capability.

Additional Sonication Resources

Learn more about the effects of sonication on alpha synuclein pre-formed fibrils (PFFs) in a webinar with StressMarq President & CEO Ariel Louwrier.

Learn about the different varieties of alpha synuclein and tau protein constructs and their characteristics, as well as the effects of sonication on preformed fibrils (PFFs).

References

1. Polinski, Nicole K et al. “Best Practices for Generating and Using Alpha-Synuclein Pre-Formed Fibrils to Model Parkinson’s Disease in Rodents.” Journal of Parkinson’s disease vol. 8,2 (2018): 303-322. doi:10.3233/JPD-171248.
2. Saraceno, C., Musardo, S., Marcello, E., Pelucchi, S., & Di Luca, M. (2013). Modeling Alzheimer’s disease: from past to future. Frontiers in pharmacology, 4, 77. https://doi.org/10.3389/fphar.2013.00077.
3. Tarutani, A., Suzuki, G., Shimozawa, A., Nonaka, T., Akiyama, H., Hisanaga, S., & Hasegawa, M. (2016). The Effect of Fragmented Pathogenic α-Synuclein Seeds on Prion-like Propagation. The Journal of biological chemistry, 291(36), 18675–18688. https://doi.org/10.1074/jbc.M116.734707.