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The Virtual Journal of Nanotechnology Environment, Health and Safety

HOT PAPER: Nucleation of protein fibrillation by nanoparticles,” Linse, S., C. Cabaleiro-Lago, Xue, W.-F., Lynch, I., Lindman, S., Thulin, E., Radford, S. E., Dawson, K. A. (2007). Proceedings of the National Academy of Sciences of the United States of America 104(21) 8691-8696 May 22, 2007.

This work explores the role that nanoparticles play in accelerating the rate of a process called protein fibrillation, which has been linked to amyloid diseases. Amyloid diseases are a broad class of ailments that result when amyloid proteins misfold and form insoluble fibrous plaques (fibrils) that deposit in the tissues of the body. Linse et al. noted an increased rate of protein fibrillation when beta 2-microglobulin, an amyloid protein associated with complications from kidney dialysis, was put into solution with nanoparticles. Four different types of nanoparticles (copolymer particles of N-iso-propylacrylamide (NIPAM) and N-tert-butylacrylamide (BAM), cerium oxide particles, CdSe or CdSe/ZnS quantum dots and multi-walled carbon nanotubes) each accelerated the production of small seeds upon which fibrils form most effectively. However this study did not determine that nanoparticles can cause human disease. 

Commentary paper: "Nanoparticles as catalysts for protein fibrillation" Colvin, Vicki L. and Kulinowski, Kristen M. (2007). Proceedings of the National Academy of Sciences of the United States of America 104(21) 8679-8680, May 22, 2007.

Backgrounder: For a general overview on nanoparticles and amyloid diseases, see here.

For Questions and Answers about nanoparticles and amyloid diseases, see here.




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This work is supported in part by the Nanoscale Science and Engineering Initiative of the National Science Foundation
under NSF Award Number EEC-0118007.

 
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