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  EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers

Ehrnhoefer, D. E., Bieschke, J., Boeddrich, A., Herbst, M., Masino, L., Lurz, R., et al. (2008). EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nature Structural & Molecular Biology, 15(6), 558-56. doi:10.1038/nsmb.1437.

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Genre: Journal Article
Alternative Title : Nat Struct Mol Biol

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Ehrnhoefer, Dagmar E, Author
Bieschke, Jan, Author
Boeddrich, Annett1, Author              
Herbst, Martin, Author
Masino, Laura, Author
Lurz, Rudi2, Author
Engemann, Sabine, Author
Pastore, Annalisa, Author
Wanker, Erich E, Author
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1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              
2Max Planck Society, ou_persistent13              

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 Abstract: The accumulation of beta-sheet–rich amyloid fibrils or aggregates is a complex, multistep process that is associated with cellular toxicity in a number of human protein misfolding disorders, including Parkinson's and Alzheimer's diseases. It involves the formation of various transient and intransient, on- and off-pathway aggregate species, whose structure, size and cellular toxicity are largely unclear. Here we demonstrate redirection of amyloid fibril formation through the action of a small molecule, resulting in off-pathway, highly stable oligomers. The polyphenol (- )-epigallocatechin gallate efficiently inhibits the fibrillogenesis of both alpha-synuclein and amyloid-beta by directly binding to the natively unfolded polypeptides and preventing their conversion into toxic, on-pathway aggregation intermediates. Instead of beta-sheet–rich amyloid, the formation of unstructured, nontoxic alpha-synuclein and amyloid-beta oligomers of a new type is promoted, suggesting a generic effect on aggregation pathways in neurodegenerative diseases.

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Language(s): eng - English
 Dates: 2008-05-30
 Publication Status: Published in print
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Title: Nature Structural & Molecular Biology
  Alternative Title : Nat Struct Mol Biol
Source Genre: Journal
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Pages: - Volume / Issue: 15 (6) Sequence Number: - Start / End Page: 558 - 56 Identifier: ISSN: 1545-9993