| 研究実績の概要 |
Aberrant Protein aggregation is essential for more than 30 serious diseases, such as Alzheimer's disease and type Ⅱ diabetes. A better understanding of the mechanism leading to protein aggregation is very important for the treatment and prevention of these diseases. In my previous study, I constructed phase diagrams of lysozyme to explain the role of solubility and supersaturation in alcohol-induced lysozyme aggregation. Cytochrome c aggregation was investigated in the same system this year for deepening the understanding of protein aggregation.
Apocytochrome c and Ag-apocytchrome c were prepared from holocytochrome c using silver sulfate method. Then, the aggregation behavior of three types of cytochrome c were examined in water/alcohol mixtures. Based on the results, phase diagrams of three types of cytochrome c were contrasted. By comparing the phase diagrams, we found that cytochrome c might be inherently low amyloidogenic, and removing heme group decreased cytochrome c solubility, widening the amoprphous region. My results further suggested that protein aggregation was not correlated with protein secondary structure content.
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| 今後の研究の推進方策 |
I examined the aggregation behavior of two model globular proteins, lysozyme and cyotchrome c, in water/alcohol mixtures, and constructed their phase diagrams depending on the results. I will study the aggregation of intrinsically disordered proteins in the next. Amyloid β(1-40) and α-synuclein will be employed because of their close association with Alzheimer's disease and Parkinson's disease.
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