ULTRASOUND DRIVEN AMYLOID FIBRIL UNFOLDING INVESTIGATED BY MOLECULAR MODELLING

Alzheimer's disease (AD) is the most common type of dementia. This pathology is characterized by an abnormal aggregation of misfolded proteins into plaques, causing proximal neurons death. Many pharmacological strategies have been proposed to target amyloid aggregation, but regrettably many of them have shown to be ineffective. Ultrasound based technique has shown to be a valid nonpharmacological strategy to reduce plaque size. In this connection, it has been observed that stable cavitation phenomena related to ultrasound can affect protein secondary structures. Modelling techniques and in particular Molecular Dynamics (MD) can provide an adequate tool to observe biological phenomena with fine space (nanometers) and time (nanoseconds) resolution. The aim of this work is to shed light on molecular mechanisms driving the amyloid fibril unfolding during cavitation.