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Science 14 January 2005:
Vol. 307. no. 5707, p. 177
DOI: 10.1126/science.307.5707.177p
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This Week in Science
Amyloid fibrils form by aggregation of diverse peptides and proteins and are involved in protein folding disorders such as Alzheimer's and prion diseases. Now Petkova et al. (p. 262) show that the morphology of fibrils formed by the beta-amyloid peptide associated with Alzheimer's disease, can be controlled experimentally by variations in fibril growth conditions. Morphological differences correlated with specific differences in molecular structure, and both morphology and molecular structure propagated in a "heritable" manner when fibrils were grown in vitro from pre-formed seeds. The different fibril morphologies possessed significantly different toxicities in neuronal cell cultures. Thus, certain amyloid morphologies may prove to be more pathogenic than others in amyloid diseases.
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Science. ISSN 0036-8075 (print), 1095-9203 (online)
