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Designed Short Peptides that Form Amyloid‐Like Fibrils in Coassembly with Amyloid β‐Peptide (Aβ) Decrease the Toxicity of Aβ to Neuronal PC12 Cells
Author(s) -
Suzuki Miho,
Takahashi Tsuyoshi,
Sato Junichi,
Mie Masayasu,
Kobatake Eiry,
Mihara Hisakazu
Publication year - 2010
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000181
Subject(s) - peptide , amyloid (mycology) , fibril , amyloid fibril , chemistry , p3 peptide , amyloid β , toxicity , biochemistry , β amyloid , biophysics , amyloid precursor protein , biology , medicine , alzheimer's disease , pathology , organic chemistry , disease , inorganic chemistry
Fine‐tuning peptides: Designed short peptides bearing an unnatural amino acid at position 6 or 7 coassembled with toxic amyloid β‐peptide (Aβ) oligomers afford less toxic amyloid‐like fibrils. The greater aggregation capabilities of the designed peptides resulted in dramatic decreases in the toxic and apoptotic activities of Aβ oligomers towards PC12 cells.