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.

Note to the Editor: VIB, the Flanders Interuniversity Institute for Biotechnology, is a research institute where 800 scientists conduct gene technological research in a number of life-science domains, such as human health care and plant systems biology. Through a joint venture with four Flemish universities (Ghent University, the Catholic University of Leuven, the University of Antwerp, and the Free University of Brussels) and a solid funding program for strategic basic research, VIB unites the forces of nine university science departments in a single institute. Through its technology transfer activities, VIB strives to convert the research results into products for the benefit of consumers and patients. VIB also distributes scientifically substantiated information about all aspects of biotechnology to a broad public.