Protein fibrillation and what to do about it
Prof. Daniel Otzen, Department of Life Sciences, Aalborg University
Newly appointed Adjoint Professor at the Biomacromolecules-Group, Department of Pharmaceutics and Analytical Chemistry, The Danish University of Pharmaceutical Sciences
Thursday, August 24th, 2006 10.00 in Benzon Auditorium
The Danish University of Pharmaceutical Sciences Universitetsparken 2, 2100 Copenhagen O
Abstract
Most proteins can under (un)suitable conditions aggregate to form needle-shaped structures called fibrils or amyloid. The aggregation process is a multistep mechanism which involves the formation of increasingly complex structures. The early stages (which often appear to have a ring-like structure by electron microscopy) appear to be the most cytotoxic and may be the causative agent in diseases such as Parkinson's and Alzheimer's disease. Using a number of test cases including dendrimers as examples, I will present research in my group devoted to elucidating the molecular mechanisms behind aggregation and discuss what strategies can be used to combat this highly unwanted process.
