The Sample Preparation And The Structure Preliminary Studies Of Two Amyloid Fibrils Protein

Neurodegenerative diseases such as Alzheimer’s(AD), Parkinson’s (PD), prion disorders, Huntington’s (HD) disease and ALS are characterised by a loss of neurons in specific regions of the brain and spinal cord. Yet,there is no effective therapeutic method for these diseases at present. Intracellular or extracellular inclusion is present in the pathological regions, and the pathogenesis is similar among different kinds of neurodegenerative diseases. The protein secondary structure transforms from a-helix to p-sheet in the process of amyloid fibrosis. Each amyloid protein has a core sequence, which plays a key role in the pathological mechanism.In this work, we prepare the protein sample HC and NAC with biological method successfully, which reduced the research cost compared with Chemical synthesis method. Then we detact that the protein secondary structure transforms from a-helix to β-sheet in the process of amyloid fibrosis, and it proves that HC and NAC are critical fraction for the pathology. Besides,We also try to use solid state NMR technique to analyse the detailed three-dimensional structure of the two protein.