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Interaction between synthetic amyloid-β-peptide (1–40) and its aggregation inhibitors studied by electrospray ionization mass spectrometry

✍ Scribed by Zsolt Skribanek; Lajos Baláspiri; Marianna Mák

Publisher
John Wiley and Sons
Year
2001
Tongue
English
Weight
104 KB
Volume
36
Category
Article
ISSN
1076-5174

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✦ Synopsis

Abstract

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.

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