Premium
Alzheimer β‐amyloid peptides: Structures of amyloid fibrils and alternate aggregation products
Author(s) -
Gorman Paul M.,
Chakrabartty Avijit
Publication year - 2001
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/1097-0282(2001)60:5<381::aid-bip10173>3.0.co;2-u
Subject(s) - fibril , fibrillogenesis , chemistry , senile plaques , amyloid fibril , amyloid (mycology) , neurodegeneration , peptide , biophysics , amyloidosis , p3 peptide , biochemistry , amyloid β , alzheimer's disease , amyloid precursor protein , pathology , disease , biology , medicine , inorganic chemistry
The amyloidoses are a heterogeneous group of diseases, which are characterized by the local or systemic deposition of amyloid. At the root of these diseases are changes in protein conformation where normal innocuous proteins transform into insoluble amyloid fibrils and deposit in tissues. The amyloid fibrils of Alzheimer's disease are composed of the Aβ peptide and deposit in the form of senile plaques. Neurodegeneration surrounds the amyloid deposits, indicating that neurotoxic substances are produced during the deposition process. Whether the neurotoxic species is the amyloid fibril or a fibril precursor is a current area of active research. This review focuses on advancements made in elucidating the molecular structures of the Aβ amyloid fibril and alternate aggregation products of the Aβ peptide formed during fibrillogenesis. © 2002 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 60: 381–394, 2001