β‐Cyclodextrin interacts with the Alzheimer amyloid β‐A4 peptide
- 21 March 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 341 (2-3) , 256-258
- https://doi.org/10.1016/0014-5793(94)80467-2
Abstract
Electrospray ionisation mass spectrometry has been used to show that the synthetic 40 amino acid β-amyloid peptide (β1-40) interacts with the cyclic oligosaccharide β-cyclodextrin. This interaction, presumably with the hydrophobic aromatic moieties on the peptide, has been shown to diminish substantially the neurotoxic effects of β1-40 in a cell line.Keywords
This publication has 11 references indexed in Scilit:
- Analysing the complexation of amino acids and peptides with β‐cyciodextrin using electrospray ionization mass spectrometryRapid Communications in Mass Spectrometry, 1993
- Recombinant-DNA-derived insulin analogues as potentially useful therapeutic agentsTrends in Biotechnology, 1993
- A 109-amino-acid C-terminal fragment of Alzheimer's-disease amyloid precursor protein contains a sequence, -RHDS-, that promotes cell adhesionBiochemical Journal, 1992
- In vitro aging of ß-amyloid protein causes peptide aggregation and neurotoxicityBrain Research, 1991
- Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's diseaseJournal of Molecular Biology, 1991
- Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin NeuropeptidesScience, 1990
- Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation.Journal of Histochemistry & Cytochemistry, 1989
- Neurotoxicity of a Fragment of the Amyloid Precursor Associated with Alzheimer's DiseaseScience, 1989
- Amyloid plaque core protein in Alzheimer disease and Down syndrome.Proceedings of the National Academy of Sciences, 1985
- Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid proteinBiochemical and Biophysical Research Communications, 1984