Paper presented at the 19th Informal Meeting on Mass Spectrometry, Noszvaj, Hungary, 29 April–3 May 2001.
Interaction between synthetic amyloid-β-peptide (1–40) and its aggregation inhibitors studied by electrospray ionization mass spectrometry†
Version of Record online: 1 NOV 2001
Copyright © 2001 John Wiley & Sons, Ltd.
Journal of Mass Spectrometry
Volume 36, Issue 11, pages 1226–1229, November 2001
How to Cite
Skribanek, Z., Baláspiri, L. and Mák, M. (2001), Interaction between synthetic amyloid-β-peptide (1–40) and its aggregation inhibitors studied by electrospray ionization mass spectrometry. J. Mass Spectrom., 36: 1226–1229. doi: 10.1002/jms.243
- Issue online: 12 NOV 2001
- Version of Record online: 1 NOV 2001
- Manuscript Accepted: 4 OCT 2001
- Manuscript Received: 8 MAY 2001
- Gedeon Richter Ltd
- amyloid-β-peptide (1–40);
- aggregation inhibitors;
- protein–ligand interactions;
- electrospray ionization mass spectrometry
It is generally postulated that amyloid-β-peptides play a central role in the progressive neurodegeneration observed in Alzheimer's disease. Important pathological properties of these peptides, such as neurotoxicity and resistance to proteolytic degradation, depend on the ability of amyloid-β-peptides to form β-sheet structures and/or amyloid fibrils. Amyloid-β-peptides are known to aggregate spontaneously in vitro with the formation of amyloid fibrils. The intervention on the amyloid-β-peptides aggregation process can be envisaged as an approach to stopping or slowing the progression of Alzheimer's disease. In the last few years a number of small molecules have been reported to interfere with the in vitro aggregation of amyloid-β-peptides. Melatonin, a hormone recently found to protect neurons against amyloid-β-peptide toxicity, interacts with amyloid-β-peptide (1–40) and amyloid-β-peptide (1–42) and inhibits the progressive formation of β-sheet and/or amyloid fibrils. These interactions between melatonin and the amyloid peptides have been demonstrated by circular dichroism (CD) and electron microscopy for amyloid-β-peptide (1–40) and amyloid-β-peptide (1–42) and by nuclear magnetic resonance (NMR) spectroscopy for amyloid-β-peptide (1–40). Our electrospray ionization mass spectrometric (ESI-MS) studies also proved that there is a hydrophobic interaction between amyloid-β-peptide (1–40) and melatonin and the proteolytic investigations suggested that the interaction took place on the 29–40 amyloid-β-peptide segment. The wide-ranging application of these results would provide further information and help in biological research. Copyright © 2001 John Wiley & Sons, Ltd.