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Despite the large and growing prevalence of AD, there exists no single diagnostic for confirming its onset nor any agent that effectively prevents its progression. NeuroDelta believes their novel technology will make them the first to achieve both.

The progressive loss of cognitive function, characteristic of AD, is accompanied by two disease-associated changes in the brain. One of the changes involves formation of plaques in the space between neuronal cells, composed primarily of amyloid-β (a protein in the brain). The second change involves the deformation of another brain protein, tau, which normally regulates the function of neurons. The deformation of tau results in the formation of Neurofibrillary Tangles (NFTs), which are insoluble, twisted fibres that build up inside the neuronal cells.

Although numerous theories abound regarding disease pathology, amyloid-β and its role in plaque formation has become central to AD research and is believed to be a critical target for eventual treatment. After noting that phosphorylation defects were a major pathological feature of AD, NeuroDelta scientists discovered that amyloid-β itself could be phosphorylated, and that this form was significantly more toxic to neuronal cells. This discovery represents a completely new approach to AD research, and seeks to explain both plaque and NFT formation in the AD brain. NeuroDelta is the only company looking at this unique protein modification and holds international patent protection.

NeuroDelta's theory is that amyloid-β becomes phosphorylated inside the neuronal cells of AD patients. This modification causes the compound to become highly toxic, killing neurons. As a result of the neuronal damage, amyloid-β plaques build up around the dead cells, which is a normal response to cell death. NeuroDelta also believes that not all Amyloid-plaques are toxic, but that phosphorylated amyloid-β plays a direct role in the formation of the toxic species, which cause further neural degeneration.

NeuroDelta also noted that the levels of phosphorylating-enzymes (kinases) are elevated in the AD brain, and believe that amyloid-β itself may play a role in activating the kinase. These kinases could contribute to the other major pathological feature of AD, playing a downstream role in the phosphorylation of the tau protein, resulting in NFT s and further neural damage. The increased levels of kinase activity also promote the continued phosphorylation of amyloid-β, thus continuing the cyclic effect.

Though many questions remain unanswered, the identification of phosphorylated amyloid-β and its role in AD pathology offers an exciting new area of potential therapies that NeuroDelta intends to exploit.