Lead Partner: University College Dublin
At University College Dublin we have developed an ultra-high resolution atomic force microscope for aqueous operation that has enabled us to investigate the role of water and ions in biological function by directly imaging water structure and ion charge distribution with unprecedented resolution (e.g. http://pubs.acs.org/doi/pdfplus/10.1021/ja2068142). We now offer two PhD studentships to further apply this new AFM capability to investigate functional protein aggregation at interfaces and protein interactions at the membrane-fluid interface specifically. While amyloid protein aggregation is frequently associated with incurable diseases of aging such as Alzheimer’s and Parkinson’s disease it also plays a functional role in many natural materials including adhesives, biofilms and hydrophobic coatings opening up the possibility of developing new biomaterials via the process of biomimicry (e.g. The Functional Fold: Amyloid Structures in Nature [http://www.crcpress.com/product/isbn/9789814267403], Pan Stanford Publishing). To date the study of amyloid based natural materials has primarily focussed on their identification and characterisation. We intend to utilise the subnanometer sensitive of our AFM to understand initial amyloid formation at the molecular level and the role played by the adjacent interface in this process. We will also explore the role of water and ions in mediating the interactions of proteins at the membrane-fluid interface.