Abstract

Amyloid plaques, as found in the organs of individuals suffering from a number of degenerative diseases, are found mainly to constitute fibrous protein aggregates. These aggregates may be made in vitro from almost any protein, or poly-peptide not limited to the disease-causing ones. The structure formed is very stable and resistant to relatively harsh conditions.

In this study we aim to investigate the following key points: -

What is the plasticity of the amyloid structure to chemical modification with small molecules?

What are the effects of incorporating small molecules into the fibrils? Both on the fibril structure and the label molecule.

Is any ordering induced in the arrangement of the label molecules upon fibrilisation?

Is there any delocalisation of excitons over a number of dye molecules?

Can we make macromolecular equivalents of di-block co-polymers that display features such as exciton migration and trapping or semi-conducting effects?

Numerous spectroscopic techniques are employed, including steady-state and time-resolve fluorescence methods and circular dichroism, FTIR and raman spectroscopy. A number of microscopic techniques are also used, such as AFM , SNOM and confocal microscopy.

This work shows that additional groups, with interesting properties, can be successfully incorporated into the amyloid structure. Using appropriate groups could lead to some useful and novel nano-materials.