Protein nanofibrils from whey can be used to produce foams (aerogels). These foams have the facinating behavior of becoming stronger and stronger during incubation at temperatures that melt many other polymers. The foams also remain intact in harsh environments such as DTT+SDS+ 6M urea and in hot oil or diesel. Maybe proteins can be the future material of choice for high temperature applicatins? The works was done in collaboration with Mikael Hedenqvist's group and is published in Advances Sustainable Systems.
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.
Degree Project in Engineering Chemistry, First Cycle (KA103X), teacher, assistant | Course web