"Knowing what the enemy looks like provides us with better tools to fight it. It's a very shrewd and sneaky adversary because it combines a compact nucleus with a diffuse shell," says Professor Otzen. "We haven't yet found its Achilles heel, but we've gained a much better starting point for interpreting what happens, and understanding the substances that can bind to the oligomers. We'll be able to study whether there are substances that can jog the distribution of oligomers, for example, so that they 'suppress' the formation of the toxic oligomers and boost the formation of the harmless type that can go on to become fibrils," he concludes. This knowledge is useful in the work to develop pharmaceuticals and in the understanding of Parkinson's disease. The research can be better targeted, but based on the slogan that the more you know, the more complex things can often be. Even though we know the enemy, we do not yet know how to nail it.
The existential aspect
Back to the question of the existential aspect, because conditions like Parkinson's disease are to a great extent an expression of human progress and well-being.
What is so special about oligomers is that they have no purpose in the body. They are not designed to do anything in particular. Protein aggregation is basically an expression of a system error in the body that shows the system is getting old and tired. This means there is not necessarily a simple explanation of why the oligomers occur. In a way, they are the shady side of the proteins' ability to make beautiful structures because this also provides them with an opportunity to make wrong structures.<
|Contact: Daniel Otzen|