Analysis of Biomolecular Condensates in Neurodegenerative Diseases
Abnormal forms of biomolecular condensates are associated with many human diseases. Our experts are dedicated to the broad characterization of pathological condensates, opening up exciting new avenues for therapeutic intervention. Here, CD BioSciences offers professional services to analyze biomolecular condensates as therapeutic targets for neurodegenerative diseases.
Research Progress of Biomolecular Condensates in Neurodegenerative Diseases
Protein misfolding and abnormal accumulation typically occur in neurodegenerative diseases. Pathological transitions in biomolecular condensates can trigger the nucleation and polymerization process of misfolded protein aggregation, and the promotion of protein accumulation in neurodegenerative disease deposits. Compelling evidence for condensate-related diseases has emerged in neurodegeneration, and LLPS may contribute to the pathogenesis of age-related neurodegenerative diseases such as amyotrophic lateral sclerosis, frontotemporal dementia, and Alzheimer's disease.
Fig. 1. Proteins associated with neurodegenerative diseases show LLPS behavior. (Zbinden A, et al., 2020)
Customized Services
Many of the proteins that make up neurodegenerative condensates of the disease contain low-complexity and/or disordered structural domains, and have been shown to be phase-separated under physiological conditions. However, the mechanistic link between LLPS of these proteins and neurodegeneration is still not fully understood. As one of the leading service providers of biomolecular condensates, CD BioSciences offers services to analyze the intrinsic drivers and regulators of LLPS in proteins associated with neurodegenerative diseases.
We have cutting-edge technology to monitor the phase transition of biomolecular condensates from liquid to solid during several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), Huntington's disease (HD), tau proteinopathy and synaptophysis. In addition, we provide multicellular or animal models to establish higher order systems in vitro and at the cellular level to analyze the material properties and dynamics of biomolecular condensates that reflect the actual pathophysiology of neurodegenerative diseases.
A large number of proteins associated with neurodegenerative diseases have been shown to undergo LLPS in vitro and in vivo. Here, we focus on several proteins where this association appears to be particularly strong, including TAR DNA binding protein 43 kDA (TDP-43), Fused in sarcoma (FUS), Tubulin associated unit (Tau), and α-synuclein. If you would like to analyze other biomolecular condensates associated with neurodegenerative diseases (such as Heteronuclear RNA-binding protein A1, T-cell intracellular antigen 1, etc.), you can contact us directly for a customized service. The services we can provide include, but are not limited to:
CD BioSciences offers proven models and technologies to analyze the physiological role of LLPS and the regulatory mechanisms of the proteins involved in neurodegenerative diseases. We aim to help our clients analyze the key molecules responsible for pathology and develop new therapeutic approaches for these still incurable neurodegenerative diseases. If you have any special requirements for our services, please feel free to contact us. We are looking forward to working together with your attractive projects.
Reference
- Zbinden A, et al. (2020) Phase separation and neurodegenerative diseases: a disturbance in the force[J]. Developmental cell, 55(1): 45-68.
For research use only, not intended for any clinical use.
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