Noncovalent interaction between amyloid-β-peptide (1-40) and oleuropein studied by electrospray ionization mass spectrometry

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作者：
Bazoti, Fotini N. [1 ,4 ]
Bergquist, Jonas [2 ]
Markides, Karin E. [2 ]
Tsarbopoulos, Anthony [1 ,3 ,4 ]
机构：
[1] Department of Pharmacy, Laboratory of Pharmaceutical Analysis, University of Patras, Rio, Greece
[2] Department of Analytical Chemistry, Biomedical Center, Uppsala University, Uppsala, Sweden
[3] GAIA Research Center, Goulandris Natural History Museum, 13 Levidou str., Kifissia 145 62, Greece
[4] GAIA Research Center, Goulandris Natural History Museum, Kifissia, Greece
来源：
Journal of the American Society for Mass Spectrometry | 2006年 / 17卷 / 04期
关键词：
Beta amyloid peptide (Aβ) is the major proteinaceous component of senile plaques formed in Alzheimer's disease (AD) brain. The aggregation of Aβ is associated with neurodegeneration; loss of cognitive ability; and premature death. It has been suggested that oxidative stress and generation of free radical species have implications in the fibrillation of Aβ and its subsequent neurotoxicity. For this reason; it is proposed that antioxidants may offer a protective or therapeutic alternative against amyloidosis. This study is the first report of the formation of the noncovalent complex between Aβ or its oxidized form and the natural derived antioxidant oleuropein (OE) by electrospray ionization mass spectrometry (ESI MS). ESI MS allowed the real time monitoring of the complex formation between Aβ; OE; and variants thereof. Several experimental conditions; such as elevated orifice potential; low pH values; presence of organic modifier; and ligand concentration were examined; to assess the specificity and the stability of the formed noncovalent complexes. © 2006 American Society for Mass Spectrometry;
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页码：568 / 575
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