Computational modelling of graphene oxide and amyloidogenic protein amylin

Detailed understanding of the interactions between nanomaterials and biological molecules is crucial for the development of novel materials in modern medicine for targeted drug delivery and novel therapeutics. On the other hand, the incorporation of various nanomaterials into everyday life is equally as progressive, which could lead to potential adverse implications on biological systems. Recent studies have suggested that some carbon-based nanoparticles can promote, and others can inhibit fibril formation of amyloidogenic peptides and proteins. These types of proteins can misfold and aggregate leading to the accumulation of insoluble fibril-like structures, which have been linked to diseases such as Alzheimer's, atherosclerosis and type-II diabetes. The mechanisms of interactions that render these nanomaterials as inhibiting or promoting of amyloid formation remain unclear. However, with the aid of advanced computational resources, it is now possible to explore the conformational features and dynamical interactions of proteins with complex nanomaterials at atomistic details and time scales inaccessible by experiments. In order to explore the interactions of proteins with nanomaterials it is important we have a detailed understanding of the dynamical behaviour and properties of the individual systems first. With this in mind, theoretical computational approaches were utilised to investigate the structures and dynamics of the amyloidogenic protein amylin and Graphene Oxide (GO).