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Misfolded Protein Interaction Analysis Service Based on SPR Technology
Neurodegenerative diseases have become a worldwide problem in the later years of life of middle-aged and elderly people. Despite the increasing number of researchers involved in the development of drugs for neurodegenerative diseases, there are still no effective treatments available. The study of disease mechanisms is the first step in disease research. It is now known that progressive neuronal death is a common feature of all neurodegenerative diseases, such as Parkinson's disease, Alzheimer's disease and Huntington's disease, which leads to neurological dysfunction. Although these diseases can present clinically with different symptoms, they are all caused by protein misfolding.
Fig.1 Aβ plaques accelerate tau spreading and cognitive decline in human Alzheimer's disease(Busche, M. A.; et al, 2020)
Protein folding is the process by which a protein acquires its functional structure and conformation. According to the principles of thermodynamics and kinetics, through this physical process, proteins fold from irregular coiling into a specific functional three-dimensional structure. In translation from mRNA sequences into linear peptide chains, proteins are in the form of defolded polypeptides or irregular coils. When proteins fold correctly, they function normally. When proteins are misfolded, they lead to disease.
The pathogenesis of Alzheimer's disease is complex and has yet to be fully deciphered. As shown above, the prevailing view is that progressive deposition of extracellular β-amyloid (Aβ) and aggregation of intracellular tau proteins in the brain lead to neuronal death and cognitive impairment.
- Deposition of extracellular β-amyloid leads to the formation of age spots.
- Hyperphosphorylated tau protein leads to the disintegration of neuronal microtubules, disrupting the cytoskeleton and signal transduction processes.
- Other factors including neuroinformation, oxidative stress, cholinergic deficiency, mitochondrial dysfunction and autophagy dysfunction also play an important role in disease progression.
Surface plasmon resonance (SPR) in the process of misfolded protein interaction analysis
The study of neurological disorders is a hot area of biology at the moment, with complex mechanisms and no specific drugs available. As we have seen above, protein misfolding is a major cause of neurological disorders, so research into neurological disorders has focused on misfolded proteins. Misfolding of proteins affects their normal physiological function and results in disease. The analysis of protein-related interactions is integral to the mechanistic study of neurological disorders, which is part of basic research and the basis for the development of neurological drugs. If you have a research need in this area, Creative Proteomics can provide you with high-throughput intermolecular interaction analysis services through the SPR technology platform. Compared to conventional interaction analysis instruments, SPR can greatly improve the efficiency of analysis while maintaining accuracy.
Fig.2 BIAchip™ in the process of misfolded protein interaction analysis
Firstly, SPR technology can provide high throughput analysis of biomolecular interactions, helping you to explain the mechanisms of neurological diseases at the molecular level. This technology enables the simultaneous analysis of hundreds or thousands of samples in a single run.
Secondly, the analysis of the mechanisms of neurological diseases provides therapeutic targets and ideas for the development of specific drugs for neurological diseases. The SPR technology platform can provide you with high-throughput screening of targets and lead compounds in your drug discovery centre, which can greatly facilitate the development of new drugs.
Choosing SPR technology platform of Creative Proteomics, you will greatly save time and money costs owing to high-throughput intermolecular interaction detection. All services are available on a 24/7/365 basis. If you have any questions or suggestions about SPR, please feel free to contact us right now.
Reference
- Busche, M. A.; et al. Synergy between amyloid-β and tau in Alzheimer's disease. Nature Neuroscience. 2020, 1754(1-2): 200–209.
For research use only. Not intended for any clinical use.