New directions of research focus on protein folding and mechanisms of secondary structure formation in biological polymers. Protein aggregation into a variety of apparently generic supramolecular structures is being studied to look for quasi-universal responses, treating misfolded/partially-folded proteins as monomers with specific interactions. The structure and kinetics of amyloid fibril formation is important in understanding the progression of neurodegenerative diseases such as Alzheimer's disease. Any insight into the processes at work eventually promises a better understanding of the etiology of the disease and might suggest alternative therapeutic approaches.
Classical polymer physics has a new life in our group. New theoretical approaches allow progress in previously intractable areas such as swelling of gels and glassy dynamics. In experiment, we utilise new techniques to address old problems of stress relaxation, time-temperature superposition and scaling. These model systems also allow the development of an improved understanding of living matter.
Based on the expertise present in BSS we try to identify the essential functional features of biological tissues (biomechanical properties of normal and diseased tissue; optical properties of the retina) and recreate them in biomimetic structures. By this approach we expect to be able to produce artificial 3D polymer matrices to better study physiological cell growth or to reduce the foreign-body reaction encountered with traditional neural implants.