An interaction of β‐amyloid with aluminium in vitro
- 21 June 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 324 (3), 293-295
- https://doi.org/10.1016/0014-5793(93)80137-j
Abstract
We have used circular dichroism spectroscopy to confirm that, in a membrane‐mimicking solvent, AβP(1–40) adopts a partially helical conformation and we have demonstrated the loss of this structure in the presence of physiologically relevant concentrations of aluminium. This is the first evidence of a direct biochemical interaction between aluminium and β‐amyloid and may have important implications for the pathogenesis of Alzheimer's disease.This publication has 10 references indexed in Scilit:
- Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum.Proceedings of the National Academy of Sciences of the United States of America, 1993
- The cellular toxicity of aluminiumJournal of Theoretical Biology, 1992
- Absence of aluminium in neuritic plaque cores in Alzheimer's diseaseNature, 1992
- Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease: Analysis of circular dichroism spectraJournal of Molecular Biology, 1992
- Metal ion-induced conformational changes of phosphorylated fragments of human neurofilament (NF-M) proteinJournal of Molecular Biology, 1992
- beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicityJournal of Neuroscience, 1992
- Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin NeuropeptidesScience, 1990
- ALUMINOSILICATES AND SENILE PLAQUE FORMATION IN ALZHEIMER'S DISEASEThe Lancet, 1986
- Estimation of globular protein secondary structure from circular dichroismBiochemistry, 1981
- Computed circular dichroism spectra for the evaluation of protein conformationBiochemistry, 1969