Neutron scattering analysis of the effect of RTILs on the equilibrium properties and fibrillation kinetics of amyloidogenic proteins
Supra-molecular protein structures known as amyloid fibres play a major role in neurological conditions such as Parkinson and Alzheimer, but also represent promising new materials for nanotechnology. Recent bio-chemical investigations report that the self-assembly of lysozyme into amyloid fibrils is greatly affected by the addition of room temperature ionic liquids (RTILs) to the proteins' solution, The full exploitation of these observations in pharmacology and in the nanotechnology, however, requires a better understanding of the mechanisms of action of these compounds. I propose to use Elastic and Quasi elastic neutron scattering to investigate how RTILs change the ps-to-ns dynamics of the protein and of its hydration water, thus affecting the fibrillation kinetics. Measurements will be carried out using the backscattering spectrometer IN16B. The results will enhance our understanding of protein-RTIL interactions, and clarify the role of the solvent (water) in the evolution of the system structure and stability upon the RTIL addition. Furthermore, the dynamical information provided by experiments will allow us to check/validate standard force fields used in computer simulations.
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BENEDETTO Antonio; BALLONE Pietro; EMBS Jan P and GONZALEZ Miguel Angel. (2016). Neutron scattering analysis of the effect of RTILs on the equilibrium properties and fibrillation kinetics of amyloidogenic proteins. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-599
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