Protein Aggregation in Crowded Environments

详细信息    查看全文

• 作者：Duncan A. White ; Alexander K. Buell ; Tuomas P. J. Knowles ; Mark E. Welland ; Christopher M. Dobson
• 刊名：Journal of the American Chemical Society
• 出版年：2010
• 出版时间：April 14, 2010
• 年：2010
• 卷：132
• 期：14
• 页码：5170-5175
• 全文大小：348K
• 年卷期：v.132,no.14(April 14, 2010)
• ISSN：1520-5126

文摘

The physicochemical parameters of biomolecules are the key determinants of the multitude of processes that govern the normal and aberrant behavior of living systems. A particularly important aspect of such behavior is the role it plays in the self-association of proteins to form organized aggregates such as the amyloid or amyloid-like fibrils that are associated with pathological conditions including Alzheimer’s disease and Type II diabetes. In this study we describe quantitative quartz crystal microbalance measurements of the kinetics of the growth of amyloid fibrils in a range of crowded environments and in conjunction with theoretical predictions demonstrate the existence of general relationships that link the propensities of protein molecules to aggregate with fundamental parameters that describe their specific structures and local environments.