Effect of the Disulfide Bridge and the C-Terminal Extension on the Oligomerization of the Amyloid Peptide ABri Implicated in Familial British Dementia

• Published in: Biochemistry (Easton) Vol. 40; no. 12; pp. 3449 - 3457
• Main Authors: El-Agnaf, Omar M. A, Sheridan, Joseph M, Sidera, Christina, Siligardi, Giuliano, Hussain, Rohanah, Haris, Parvez I, Austen, Brian M
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 27.03.2001
• Subjects: Amino Acid Sequence; Amyloid - chemistry; Amyloid - genetics; Amyloid - metabolism; Amyloid - ultrastructure; Binding Sites - genetics; Circular Dichroism; Coloring Agents; Congo Red - metabolism; Dementia - genetics; Dementia - metabolism; Dementia - pathology; Dimerization; Disulfides - chemistry; Humans; Kinetics; Membrane Glycoproteins; Membrane Proteins; Microscopy, Electron; Models, Molecular; Molecular Sequence Data; Peptide Fragments - chemistry; Peptide Fragments - genetics; Peptide Fragments - metabolism; Peptide Fragments - ultrastructure; Protein Structure, Secondary - genetics; Solutions; Spectroscopy, Fourier Transform Infrared; United Kingdom

Familial British dementia (FBD) is a rare neurodegenerative disorder and shares features with Alzheimer's disease, including amyloid plaque deposits, neurofibrillary tangles, neuronal loss, and progressive dementia. Immunohistochemical and biochemical analysis of plaques and vascular amyloid of...