Over the year, the University of Basel organizes many events. The themes and content of these events are as diverse as the University itself. They either address a broad public or a particular audience, such as, for example, prospective students, current students or staff. On this web page, you can find a preview of our current events.
27 Jun 2018
11:00 - 12:00
Biozentrum/Pharmazentrum, BZ 310, Klingelbergstrasse 50-70, Basel
Towards the understanding how Hsp60 inhibits neurodegenerative diseases
Vortrag von Marielle Wälti, National Institutes of Health, USA
Proteins need to obtain their 3D structure in order to function. The folding of proteins is an error prone process and often needs the help of chaperones. Moreover, missfolded states can lead to toxic aggregates such as those found in Alzheimer’s, Parkinson’s or Huntington’s disease. Hsp60 belongs to the class of the so-called chaperonins, which encapsulate their protein substrate in order to help them fold and prevent their aggregation. However, only little is known about the mechanism of how they achieve this function.
We study the interaction of the bacterial Hsp60 (GroEL) with different amyloidogenic proteins, such as a model protein, Het-s(218-289), a small fraction of the Huntingtin protein, and the Alzheimer peptides, Aß 40 and 42 at atomic resolution. Therefore, we use a combination of solution- and solid state NMR experiments with different methods such as EPR, AFM, EM, AUC and DLS. We show that the chaperone not only slows down fibril formation, but also inhibits Aß derived neurotoxicity. However, the mechanism varies among different amyloids: In the case of Het-s, we show that GroEL binds to a tail or loop of the fibrils, and accelerates protofibril formation by several orders of magnitude, but still inhibits the formation of fibrils. GroEL remains bound to Het-s throughout the entire aggregation process and decorates the fibrils in a very regular manner.
In the case of Aß, GroEL interacts with the residues found in the core of the fibril and Aß stays soluble (either monomeric or oligomeric) in presence of GroEL. We show, that the inhibition of Aß derived neurotoxicity is achieved by breaking down oligomers and aggregates and biases the equilibrium of the aggregation kinetics towards the monomer concentration.
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06 Jul 2018
12:15 - 13:15
Biozentrum/Pharmazentrum, BZ 103, Klingelbergstrasse 50-70, Basel
Molecular and cellular insights to the development and evolution of the human cerebral cortex
Vortrag von Prof. Dr. Arnold Kriegstein, University of California, San Francisco, USA
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