Studies on aggregation-propensities and secondary structural transformations of proteins
The insoluble and fibrillar aggregates of some proteins are thought to be the pathological cause of neurodegenerative 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 different 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.
GAO Yong-Guang,LI Hong-Tao,HU Hong-yu(Key Laboratory of Proteomics,Institute of Biochemistry and Cell Biology,Shanghai Institutes for Biological Sciences,the Chinese Academy of Sciences,Shanghai 200031)
HU Jun(Shanghai Institute of Applied Physics,the Chinese Academy of Sciences,Shanghai 201800;Bio-X Research Center,Shanghai Jiaotong University,Shanghai,200030)
刊 名： 核技术（英文版） SCI 英文刊名： NUCLEAR SCIENCE AND TECHNIQUES 年，卷(期)： 2005 16(1) 分类号： Q51 Q336 关键词： Aggregation-propensity Secondary structural transformation ThT fluorescence Atomic force microscopy imaging Circular dichroism spectroscopy