Z. Skribanek et al., Interaction between synthetic amyloid-beta-peptide (1-40) and its aggregation inhibitors studied by electrospray ionization mass spectrometry, J MASS SPEC, 36(11), 2001, pp. 1226-1229
It is generally postulated that amyloid-beta -peptides play a central role
in the progressive neurodegeneration observed in Alzheimer's disease. Impor
tant pathological properties of these peptides, such as neurotoxicity and r
esistance to proteolytic degradation, depend on the ability of amyloid-beta
-peptides to form beta -sheet structures and/or amyloid fibrils. Amyloid-b
eta -peptides are known to aggregate spontaneously in vitro with the format
ion of amyloid fibrils. The intervention on the amyloid-beta -peptides aggr
egation 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-beta -peptides. Melatonin, a hormone recently found to protect neu
rons against amyloid-beta -peptide toxicity, interacts with amyloid-beta -p
eptide (1-40) and amyloid-beta -peptide (1-42) and inhibits the progressive
formation of beta -sheet and/or amyloid fibrils. These interactions betwee
n melatonin and the amyloid peptides have been demonstrated by circular dic
hroism (CD) and electron microscopy for amyloid-beta -peptide (1-40) and am
yloid-beta -peptide (1-42) and by nuclear magnetic resonance (NMR) spectros
copy for amyloid-beta -peptide (1-40). Our electrospray ionization mass spe
ctrometric (BSI-MS) studies also proved that there is a hydrophobic interac
tion between amyloid-beta -peptide (1-40) and melatonin and the proteolytic
investigations suggested that the interaction took place on the 29-40 amyl
oid-beta -peptide segment. The wide-ranging application of these results wo
uld provide further information and help in biological research. Copyright
(C) 2001 John Wiley & Sons, Ltd.