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TANGO - towards faster prognosis of Alzheimer's and Parkinson's diseases?
September 13, 2004A large number of diseases - including Alzheimer's disease, Parkinson's disease, and mad cow disease - are the result of proteins that erroneously assume the wrong shape, causing them to stick to each other. This phenomenon is perceptible, but up to now it has been difficult to predict. Researchers from the Flanders Interuniversity Institute for Biotechnology (VIB) at the Free University of Brussels (VUB), in collaboration with a German research group, have developed TANGO - a statistical method that can predict the susceptibility of proteins to sticking together. Thus, for the first time, TANGO enables the prediction of risky protein alterations that underlie this group of diseases.
When protein structure goes awry
All living creatures, including humans, are made up of cells, and the vital functions within these cells are executed by proteins. The hereditary information for the production of proteins - including, among other things, their structure and length - is contained in our genes. But in order to be able to function properly, a protein must also fold itself correctly into its 3-dimensional structure. Sometimes this goes wrong and the proteins stick together, making them toxic and causing diseases like Alzheimer's.
TANGO makes prediction of faulty protein structures possible
Until recently, it was always thought that proteins stick together arbitrarily. But now it has become clear that a universal mechanism lies behind this process. Certain structural characteristics in proteins determine their susceptibility to sticking together. Using this information, Joost Schymkowitz and Frederic Rousseau have developed TANGO, a mathematical algorithm that looks at a large amount of data - including alterations of the protein and environmental factors - to indicate the degree of probability that particular proteins will stick together.
TANGO thus opens possibilities for new diagnostic techniques for diseases that are caused by proteins that stick together erroneously. The VIB researchers also expect that TANGO will enable more efficient production of proteins for medical or industrial applications. The yield of these production processes is often low, because the proteins stick to each other and are therefore difficult to purify. With TANGO, one can determine under what conditions the solubility of the therapeutic proteins is large enough to purify them easily.
Relevant scientific publications
On 12 September, Schymkowitz and Rousseau's research was published online on the website of the authoritative journal, Nature Biotechnology (www.nature.com/nbt) Fernandez-Escamilla et al.
Given that this research can raise a lot of questions for patients, we ask you to please refer questions in your report or article to the email address that VIB makes available for this purpose: patienteninfo@vib.be. Everyone can submit questions concerning this and other medically-oriented research directly to VIB via this address.
VIB - Flanders Interuniversity Institute for Biotechnology
Until recently, it was always thought that proteins stick together arbitrarily. But now it has become clear that a universal mechanism lies behind this process. Certain structural characteristics in proteins determine their susceptibility to sticking together. Using this information, Joost Schymkowitz and Frederic Rousseau have developed TANGO, a mathematical algorithm that looks at a large amount of data - including alterations of the protein and environmental factors - to indicate the degree of probability that particular proteins will stick together.
TANGO thus opens possibilities for new diagnostic techniques for diseases that are caused by proteins that stick together erroneously. The VIB researchers also expect that TANGO will enable more efficient production of proteins for medical or industrial applications. The yield of these production processes is often low, because the proteins stick to each other and are therefore difficult to purify. With TANGO, one can determine under what conditions the solubility of the therapeutic proteins is large enough to purify them easily.
Relevant scientific publications
On 12 September, Schymkowitz and Rousseau's research was published online on the website of the authoritative journal, Nature Biotechnology (www.nature.com/nbt) Fernandez-Escamilla et al.
Given that this research can raise a lot of questions for patients, we ask you to please refer questions in your report or article to the email address that VIB makes available for this purpose: patienteninfo@vib.be. Everyone can submit questions concerning this and other medically-oriented research directly to VIB via this address.
VIB - Flanders Interuniversity Institute for Biotechnology
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Vitamin B does not slow cognitive decline in Alzheimer's
A clinical trial led by Paul S. Aisen, M.D., professor of neurosciences at the University of California, San Diego School of Medicine, showed that high-dose vitamin B supplements did not slow the rate of cognitive decline in patients with mild to moderate Alzheimer disease.
Protecting patient privacy the new fashioned way
Protecting patient privacy has been recognized as the duty of health-care providers for about as long as doctors have seen patients. In 1996 that duty became a legal obligation when Congress passed the Health Insurance Portability and Accountability Act.
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