Neurological diseases include a broad range of conditions, often causing severe disability and drastically decreasing quality of life for the patients. Very prominent are neurodegenerative disorders like Alzheimer’s disease and Parkinson’s disease. These are often caused by protein misfolding and aggregation. Another major group are neuromuscular diseases, for example Charcot-Marie-Tooth disease, amyotrophic lateral sclerosis, and muscular dystrophies like the Duchenne type.
The disease mechanisms for this group are very diverse including for example translational defects, genetic disorders, or autoinflammatory reactions. Often, the aetiology of neurological diseases is not fully elucidated. Consequently, the treatment remains a major challenge and there are no therapeutic options for many highly prevalent diseases. Thus, new tools to improve the identification of disease mechanisms as well as to develop new remedies are needed.
switchSENSE® is a valuable tool to elucidate the disease mechanisms, for example by investigating aberrant protein-protein interactions induced by protein aggregation. Moreover, it facilitates the detection of conformational changes. The technology can also be utilized to optimize target identification and validation in order to accelerate the drug discovery process and improve the outcome of clinical trials in neurology.
→ investigate conformational changes and protein misfolding
→ measure affinities of small molecules binding to nucleic acids or target proteins
→ measure complex molecular interactions, e.g. ternary binding or multispecific binders
→ CMT2N-causing aminoacylation domain mutants enable Nrp1 interaction with AlaRS
2021 I PNAS (open access)
→ CMT disease severity correlates with mutation-induced open conformation of histidyl-tRNA synthetase, not aminoacylation loss, in patient cells
2019 I PNAS
→ Dissecting FOXP2 oligomerization and DNA binding
2019 I Angewandte Chemie
→ ANKRD16 prevents neuron loss caused by an editing-defective tRNA synthetase
2018 I Nature
→ Alternative stable conformation capable of protein misinteraction links tRNA synthetase to peripheral neuropathy
2017 I Nucleic Acids Research
→ heliX® Biosensors I learn more
→ heliX® Chips I learn more
→ Reagents & Consumables I learn more
→ heliOS Software I learn more
→ proFIRE® conjugation I learn more
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