We and many others are exploring amyloid-like nanofibrils in efforts to create new materials or new food. These fibrils can be produced from a variety of different resources, including many proteins that are part of common foodstuff. The structural similarity between the food-derived fibrils and those associated with disease amyloid is an obvious concern - could they trigger the aggregation of the critical disease associated proteins, such as amyloidbeta that is involved Alzheimer's disease? Fortunately, the answer to that questions seems to be'no' as we now can show that none of the 16 tested food amyloid accelerate amyloid beta aggregation. The paper was just published in Nature Scientific Reports. The results are also highlighted in KTH News (only in Swedish).
The assembly of protein molecules into nanoscale aggregates and amyloid fibrils are key events in many biochemical processes ranging from neurodegenerative disorders, such as Alzheimer’s disease, to the design of novel nanomaterials. In my research I investigate the structural properties and interactions of such protein aggregates. In particular, I am interested in the molecular mechanisms for how protein nanostructures interact with other (bio)molecules.
New materials from protein nanofibrils
Protein nanofibrils display extraordinary mechanical and functional properties and has the potential to be used as building blocks for new materials with hieracrical structures. We develop methods to produce fibrils from protein-rich and renewable sources (e.g. plant proteins) and the technology to produce new protein-based materials.
Pathological mechanisms of protein aggregates
Protein self-assembly and deposition are hallmarks of many serious diseases but the disease-causing mechanisms remain enigmatic. However, any pathological mechanism must involve interactions between the protein aggregates and other biomolecules. We explore and characterize such interactions in order to better understand what makes a protein nanostructure toxic.
Inhibitors of protein aggregation
The mechanisms of action for small molecule inhibitors of protein aggregation remain poorly understood and the development of new therapeutics against amyloid diseases is slow. Interfering with protein self-assembly is complicated and essentially different from traditional drug design. By studying the binding mechanisms of small molecules to aggregation-prone proteins we believe that we will better understand what type of molecules could be explored as drug candidates for amyloid-diseases.