Monitoring of the protein dynamics during amyloid fibril formation

Misfolded proteins and peptides can form insoluble and highly stable specific aggregates, called amyloid fibrils. Such aggregates are related to various neurodegenerative diseases, and about fifty amyloid-related diseases have been identified. Knowing how the amyloid formation occurs in general and the effect of different agents on amyloid formation/destruction can drive the development of more efficient anti-amyloid agents. Moreover, detailed structural/morphological information may help to tune the properties of complex systems with bio-macromolecules. We aim to perform a comprehensive analysis of amyloid fibril formation, with an emphasis on studying changes in protein dynamics during amyloid formation and thus complement our data about amyloid formation as well as inhibition/destruction effect of nanomaterials on protein amyloid fibrils by applying quite new but very promising method for the amyloids area, i.e. quasi-elastic neutron scattering in our investigation.In this proposal, we will investigate the dynamic properties of lysozyme protein molecules in the native state, in amyloid aggregates and after adding of fullerenes as an inhibitor/disaggregating agent.