Alcohol induced aggregation and amyloid formation in newt (Notophthalmus viridescens) acidic Fibroblast Growth Factor.

 

S. Srisailam, T. K. S. Kumar and Chin Yu

Department of Chemistry, National Tsing Hua University, Hsinchu, Taiwan.

 

A wide range of human disorder are associated with the extracellular deposition of insoluble aggregates known as amyloid fibrils. These include Alzheimer’s diseases, type II diabetes, Primary and secondary amyloidosis, and the spongiform encephalopathies such as Creutzfeldt-Jakob disease. The mechanism of amyloid formation is still unclear. Dobson and coworkers in a series of recent publications have suggested that amyloid formation is a generic property of all proteins.  To verify if amyloid formation is an inherent property of all natural proteins, herein we examine the amyloid fibril tendency of nFGF-1 which is a b-barrel protein not known to be involved in any amyloid-based diseases. Alcohol such as 2, 2, 2-trifluoroethanol (TFE) have been shown to drive proteins to form amyloid type of aggregates. In this context, we examined the effects of various organic solvents, including TFE, on the conformation of nFGF-1. 

 

 

 

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