Effect of flavonoids on the Aβ(25-35)-phospholipid bilayers interaction

被引：24

作者：

Tedeschi, Annamaria ^{[1
]}

D'Errico, Gerardino ^{[2
]}

Lauro, Maria Rosaria ^{[1
]}

Sansone, Francesca ^{[1
]}

Di Marino, Sara ^{[1
]}

D'Ursi, Anna Maria ^{[1
]}

Aquino, Rita Patrizia ^{[1
]}

机构：

[1] Univ Salerno, Dept Pharmaceut Sci, I-84084 Fisciano, Italy

[2] Univ Naples Federico II, Dept Chem, I-80126 Naples, Italy

来源：

EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY | 2010年 / 45卷 / 09期

关键词：

Amyloid peptide; EPR spectroscopy; Flavonoids; ALZHEIMERS-DISEASE; QUERCETIN; PROTEIN; FLUIDITY; PEPTIDE; BINDING;

D O I：

10.1016/j.ejmech.2010.05.056

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

Amyloid-beta peptide (A beta) is the major component of amyloid deposits found in the brain tissue of Alzheimer patients. The tendency of amyloid peptide to form amyloid plaques is known to be related to the features of the plasma membrane. Flavonoids, a group of naturally occurring molecules, exert beneficial properties to human health thanks to their antioxidant property: this property depends on their capacity to interact and permeate the cell membrane lipid bilayer. In the present research we report an Electron Paramagnetic Resonance (EPR) investigation of 2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) membranes interacting with the beta-amyloid fragment A beta(25-35), in the presence of flavonoids rutin, quercetin, naringin and naringenin. Our results, evidencing a flavonoid-dependent rigidifying effect of the bilayer, may provide the molecular basis to explain the known neuroprotective effect of flavonoid compounds. (C) 2010 Elsevier Masson SAS. All rights reserved.

引用

页码：3998 / 4003

页数：6

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