Biophysical Society Thematic Meeting - October 25-30, 2015

Polymers and Self Assembly: From Biology to Nanomaterials

Tuesday Speaker Abstracts

Exploiting Amyloid Fibrils as Functional Biomaterials Louise Serpell University of Sussex, Brighton, United Kingdom

Amyloid fibrils are known to be composed of a cross-ß structural core that is hydrogen bonded along the length of the fibre to form a highly ordered and repetitive structure. It is clear however, that side chains play an important role in driving self-assembly and strengthening the overall structure via internal interactions between the ß-sheets as well as stacking within sheets. Our work utilizes electron microscopy, X- ray fibre diffraction and biophysical and spectroscopic techniques to examine the structure of amyloid fibrils. Research into the self-assembly of short amyloidogenic peptides has provided a novel architecture in the form of a cross-ß nanotube formed by an amphipathic peptide. Our work has highlighted the important central role for the aromatic side chains phenylalanine and tyrosine in the internal interactions within the amyloid protofilament. Most recently, we have shown oxidation leads to covalent linking of the tyrosine side chains may play a very significant role in the structure and stability of amyloid fibrils in diseases including Alzheimer’s disease. We have also shown that charge interactions play an important role and recently investigated the functionalization of amyloid fibrils using the lysine residues to promote sillconisation. This presentation will focus on recent insights into the contribution of primary sequence to the architecture of the amyloid fibrils and how these extremely stable structures may be further exploited as templates for further functionalization.

- 22 -