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Previous Volume 352:722-723 February 17, 2005 Number 7 Next

	Since this article has no abstract, we have provided an extract of the first 100 words of the full text and any section headings.

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Protein aggregation seems to cause numerous neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and familial amyloid polyneuropathy and cardiomyopathy. Once initiated, the aggregation of individual proteins into amyloid fibrils is difficult to inhibit with small molecules (Figure 1), owing to the large protein surfaces involved, the plasticity of amyloid structures, and the low binding affinities of known inhibitors. A recent study, however, gives cause for hope. Gestwicki and colleagues¹ report that small, bifunctional organic molecules may sterically block the growth and adverse effects of fibrils.

View larger version (53K): [in this window] [in a new window]   Figure 1. Inhibiting A Amyloidogenesis. A amyloidogenesis involves A aggregation into spherical structures and . . . [Full Text of this Article]

 

Source Information

From the Skaggs Institute of Chemical Biology and the Department of Chemistry, Scripps Research Institute, La Jolla, Calif.

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