Scientists at Cambridge’s Department of Chemistry have been able to construct a detailed map that shows how the formation of proteins in the brain can lead to a build-up so massive that it can lead to the development of numerous brain-damaging diseases, chief among them is Alzheimer’s. In 2010, the Alzheimer’s Research Trust found that with dementia alone, it cost the UK economy E23 billion, way more than cancer and heart disease combined cost.
    Normally, proteins are made up of chemical building blocks known as amino acids, which are joined together in a code ordered by our DNA. New proteins appear as long, thin strips, which are then intricately folded to properly carry out their designated biological function. However, there are points at which the protein can ‘misfold,’ or unfold and get tangled together with other newly-made proteins. The tangles stick to one another until they number in the millions, known as amyloid fibrils, and they start the huge deposits of proteins known as plaque, which are so huge that they are insoluble.  
    When the level of plaque in the brain reaches a critical level, a chain reaction is set off, and new focal points of tendrils form. From these tendrils, a smaller number of proteins, known as toxic oligomers, can easily diffuse through membranes, effectively killing neurons, causing memory loss, and other dementia symptoms.
    This new groundbreaking information required scientists to come together, using kinetic experiments with a framework of theory. Master equations, more commonly used in the fields of chemistry and physics, aided researchers in their efforts to better understand a disease such as Alzheimer’s, and how better to fight it.

By Lauren Horne

    University of Cambridge (2013, May 20). Molecular trigger for Alzheimer's disease identified. ScienceDaily. Retrieved May 22, 2013,
    Samuel I. A. Cohen, Sara Linse, Leila M. Luheshi, Erik Hellstrand, Duncan A. White, Luke Rajah, Daniel E. Otzen, Michele Vendruscolo, Christopher M. Dobson, and Tuomas P. J. Knowles. Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism. Proceedings of the National Academy of Sciences, 2013; DOI: 10.1073/pnas.1218402110
    At Georgetown University Medical Center, tiny, almost meniscal dosage amounts of a Leukemia-inhibiting drug known as nilotinib, were being administered to lab mice in a clinical trial to see the effects of the drug on inhibiting the formation of certain proteins in the brain, which if allowed to proceed unchecked, would build up and cause any number of diseases, from Parkinson’s disease and even Alzheimer’s disease, to a lesser known disease known as Lewry body disease.
    Neurologist and senior investigator for this study, Charbel E-H Moussa, MB and PhD, head of the dementia laboratory at Georgetown University stated that when this utilized drug, nilotinib, is used to treat CML, or chronic myelogenous leukemia. When used in high enough and safe doses, it causes the cancer cells to go into a state of autophagy, pushing them to cannibalize their own organelles, which leads to the death of tumor cells.
    In the study that was performed, for the first time, cancer drugs were being utilized for a different cause. Mice in the lab that over-expressed a specific protein, known as alpha-Symuclein, were given one Milligram of nilotinib every two days. Previous testing of the drug concluded that it would get rid of the toxic protein found in the brain, the cells would go into a state of autophagy and within a matter of treatments, the lab mice treated with the drug had drastically better movement and functionality than the untreated mice.
    At the end of the experiment, Moussa hypothesized that in order for therapy of these neurological diseases to be effective, it must happen as soon as possible. Later usage may result in retardation of further extracellular formation, as well as the accumulation of intracellular proteins such as Lewy bodies, which was the whole point of using the Leukemia drug in the first place.
    Michaeline L. Hebron, Irina Lonskaya, and Charbel E.-H. Moussa. Nilotinib reverses loss of dopamine neurons and improves motor behavior via autophagic degradation of α-synuclein in Parkinson's disease models. Hum. Mol. Genet., May 10, 2013 DOI: 10.1093/hmg/ddt192
    Georgetown University Medical Center (2013, May 10). Cancer drug prevents build-up of toxic brain protein. ScienceDaily.
_  1.

A new technology, recently approved by the FDA, allows researchers to detect amyloid plaques that often suggest Alzheimer's disease.  Created by Eli Lilly, Amyvid is a drug that, when used before a PET scan, will highlight amyloid plaque in the brain.  This method is much more preferable for diagnosis than the current method of performing an autopsy. 


            A new study shows that reducing the iron levels in blood plasma may help protect the brain          from changes. There is previous evidence that there are changes in the way the  human body      handles iron and other metals (zinc, cooper) before it shows Alzheimer's symptoms. In the             study, rats are fed a high cholesterol diet which causes them to build up plaques of a protein   called beta-amyloid and develop changes in the tau proteins. The study deals with a new drug        called deferiprone which lowered the iron concentration in the blood plasma of the rabbit and the level of beta-amyloid and the tau proteins in the brain. 


              At the University of South Florida (USF) researchers have discovered that the amyloid     precursor protein (APP) which is associated with Alzheimer's Disease regulates its own growth.        This discovery has the potential to allow scientists to treat and possible prevent the disease by controlling the regulation of the protein.  Through their research at USF, it has been determined         that the growth of APP is dependent on an enzyme (BACE1) excreted by the amyloid leading to       the theory that, if the reaction between the BACE1 and APP was blocked, Alzheimer's disease             may see its end. 


              Researchers have shown that elevated pulse pressures in older humans with Alzheimer's disease    are at a higher risk to get Cerebrovascular disease. Recent studies have shown that patients with   Alzheimer's disease that have a high pulse pressure may impair the clearance of beta-amyloid            from the brain. Other studies show that high pulse pressures increases the chance of   Cerebrovascular disease which contributes to the cause of Alzheimer's disease.

           A groundbreaking new test for the early detection of Alzheimer's disease is being developed at a research facility just north of Sydney, Australia.  Currently, the only prevalent tests of such             nature are invasive and expensive.  However, the test being developed in Syndey is a cheap            blood test that checks for a change in levels of a specific protein marker over a year in order to      determine if a patient is in deed affected by the lethal disease.  The earlier Alzheimer's is      detected, the more likely it can be slowed and even stopped.

For more exciting research progress, please visit: