Abstract The fragment Aβ (25–35) of the Alzheimer's amyloid β-peptide, like its full-length
peptide Aβ (1–42), has shown neurotoxic activities in cultured cells. The conformational …

We investigated the site-specific local structure of an amyloid peptide, NH2–GSNKGAIIGLM–
COOH [Aβ (25–35)], one of the active fragments of amyloid β peptide that is known to be …

The A4 or β-peptide (39 to 43 amino acid residues) is the principal proteinaceous
component of amyloid deposits in Alzheimer's disease. Using circular dichroism (cd), we …

Current views of the role of β‐amyloid (Aβ) peptide fibrils range from regarding them as the
cause of Alzheimer's pathology to having a protective function. In the last few years, it has …

The secondary structure of amyloid βA (25-35) and its deletion analogues was studied by
circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy and molecular …

Isotope-assisted vibrational circular dichroism (VCD) investigations have been used to
probe the site specific local structure of an amyloid peptide for the first time. A seven residue …

To structurally characterize the nonaggregated state of the amyloid β peptide, which
assembles into the hallmark fibrils of Alzheimer disease, we investigated the conformation of …

In this simulation study, we present a comparison of the secondary structure of the two major
alloforms of the Alzheimer's peptide (Aβ1–40 and Aβ1–42) on the basis of molecular …

The 42 amino acid βA4 peptide is the major constituent of the senile plaques, one of the
hallmark neuropathological lesions of Alzheimer′ s disease. While C-terminally truncated …

The three-dimensional structure of amyloid β peptide (25− 35), which has neurotoxic activity,
in lithium dodecyl sulfate micelles was determined by two-dimensional 1H NMR …