摘要
The insoluble and fibrillar aggregates of some proteins are thought to be the pathological cause of neu- rodegenerative diseases. The aggregation-propensities of different types of proteins were investigated by Thioflavine T fluorescence assay and atomic force microscopy imaging. Then, the structural transformations of the proteins from aqueous state to solid state were studied by circular dichroism spectroscopy. The results indicate that proteins of dif- ferent secondary structure show variations in their aggregation-propensities, together with their various structural transformations from aqueous state to solid state. Our studies imply that the structural transformation of proteins from solution to solid state is closely associated with their aggregation-propensities, which will provide insight into the molecular mechanism of protein aggregation in neurodegenerative diseases.
The insoluble and fibrillar aggregates of some proteins are thought to be the pathological cause of neu- rodegenerative diseases. The aggregation-propensities of different types of proteins were investigated by Thioflavine T fluorescence assay and atomic force microscopy imaging. Then, the structural transformations of the proteins from aqueous state to solid state were studied by circular dichroism spectroscopy. The results indicate that proteins of dif- ferent secondary structure show variations in their aggregation-propensities, together with their various structural transformations from aqueous state to solid state. Our studies imply that the structural transformation of proteins from solution to solid state is closely associated with their aggregation-propensities, which will provide insight into the molecular mechanism of protein aggregation in neurodegenerative diseases.
基金
Supported by the National Natural Science Foundation of China (No. 30070165)
Science & Technology Committee of Shanghai
(No.0159NM078
No.03JC14081).
关键词
聚集性质
次要结构变换
原子力学显微镜成像法
周期分色光谱
蛋白质
ThT荧光
Aggregation-propensity, Secondary structural transformation, ThT fluorescence, Atomic force microscopy imaging, Circular dichroism spectroscopy
