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Shedding Light on Alzheimer's β‐Amyloid Aggregation with Chemical Tools
Author(s) -
Kapurniotu Aphrodite
Publication year - 2012
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.201100631
Subject(s) - fibril , amyloid (mycology) , peptide , biophysics , chemistry , amyloid fibril , p3 peptide , fluorescence , in vitro , amyloid β , β amyloid , alzheimer's disease , biochemistry , amyloid precursor protein , biology , disease , medicine , pathology , inorganic chemistry , physics , quantum mechanics
Early steps in self‐assembly: Kelly and co‐workers have presented a fluorescence‐based assay system that differentially detects the early oligomers and fibrils formed by the Alzheimer's disease β‐amyloid peptide, Aβ, and provided evidence that in vitro Aβ amyloidogenesis proceeds through a nucleated conformational conversion of nonfibrillar oligomers into amyloid fibrils.