Protein− protein interactions are frequently mediated by stable, intermolecular β-sheets. A
number of cytokines and the HIV Protease, for example, dimerize through β-sheet motifs …

Polymerization of the amyloid beta (Aβ) peptide into protease-resistant fibrils is a significant
step in the pathogenesis of Alzheimer's disease. It has not been possible to obtain detailed …

Aβ peptides cleaved from the amyloid precursor protein are the main components of senile
plaques in Alzheimer's disease. Aβ peptides adopt a conformation mixture of random coil, β …

Amyloid fibrils in Alzheimer's disease mainly consist of 40-and 42-mer β-amyloid peptides
(Aβ40 and Aβ42) that exhibit aggregative ability and neurotoxicity. Although the aggregates …

The conversion of the soluble, nontoxic amyloid-β (Aβ) peptide into an aggregated, toxic
form rich in β-sheets is considered a key step in the development of Alzheimer's disease …

Amyloid-β peptide (Aβ) consists of a hydrophobic C-terminal domain (residues 29-42) that
adopts β-strand conformation and an N-terminal domain (amino acids 10-24) whose …

The seven-residue peptide N-acetyl-Lys-Leu-Val-Phe-Phe-Ala-Glu-NH2, called Aβ16-22
and representing residues 16− 22 of the full-length β-amyloid peptide associated with …

Solid-state NMR measurements have been reported for four peptides derived from β-
amyloid peptide Aβ (1–42): Aβ (1–40), Aβ (10–35), Aβ (16–22), and Aβ (34–42). Of these …

Amyloidogenic deposits that accumulate in brain tissue with the progression of Alzheimer's
disease contain large amounts of the amyloid β-peptide. A small fragment of this peptide …

We describe here the use of cysteine substitution mutants in the Alzheimer disease amyloid
plaque peptide Aβ-(1-40) to probe amyloid fibril structure and stabilization. In one approach …