Solvent Effects on Self-Assembly of 1B-Amyloid Peptide

f3-amyloid peptide (A,B) is the primary protein component of senile plaques in Alzheimer's disease patients. Synthetic AP3 spontaneously assembles into amyloid fibrils and is neurotoxic to cortical cultures. Neurotoxicity has been associated with the degree of peptide aggregation, yet the mechanism of assembly of A,B into amyloid fibrils is poorly understood. In this work, Af3 was dissolved in several different solvents commonly used in neurotoxicity assays. In pure dimethylsulfoxide (DMSO), A,B had no detectable (3-sheet content; in 0.1 % trifluoroacetate, the peptide contained one-third (-sheet; and in 35% acetonitrile/0.1 % trifluoroacetate, A,B was two-thirds (-sheet, equivalent to the fibrillar peptide in physiological buffer. Stock solutions of peptide were diluted into phosphate-buffered saline, and fibril growth was followed by static and dynamic light scattering. The growth rate was substantially faster when the peptide was predissolved in 35% acetonitrile/0.1 % trifluoroacetate than in 0.1 % trifluoroacetate, 10% DMSO, or 100% DMSO. Differences in growth rate were attributed to changes in the secondary structure of the peptide in the stock solvent. These results suggest that formation of an intermediate with a high (3-sheet content is a controlling step in A(3 self-assembly.

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