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
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
收藏
页码:3998 / 4003
页数:6
相关论文
共 50 条
  • [21] Conformational Preference of Aβ25-35 and Aβ35-25 Membrane Mimicking Environments
    Sambasivam, Dhandayuthapani
    Sivanesan, Senthilkumar
    Sultana, Sayeeda
    Rajadas, Jayakumar
    PROTEIN AND PEPTIDE LETTERS, 2019, 26 (05): : 386 - 390
  • [22] Effect of β-amyloid peptide fragment 25-35 on nonselective permeability of mitochondria
    Shevtzova, EF
    Kireeva, EG
    Bachurin, SO
    BULLETIN OF EXPERIMENTAL BIOLOGY AND MEDICINE, 2001, 132 (06) : 1173 - 1176
  • [23] Toxic effect of Aβ25-35 and fullerene C60 on erythrocytes
    Solomadin, I. N.
    Marov, N. V.
    Venediktova, N. I.
    Kosenko, E. A.
    Kaminsky, Yu. G.
    BIOLOGY BULLETIN, 2008, 35 (04) : 436 - 440
  • [24] Amyloid Beta-Peptide 25-35 (Aβ25-35) Induces Cytotoxicity via Multiple Mechanisms: Roles of the Inhibition of Glucosylceramide Synthase by Aβ25-35 and Its Protection by D609
    Tang, Zhihui
    Motoyoshi, Kaisei
    Honda, Takuya
    Nakamura, Hiroyuki
    Murayama, Toshihiko
    BIOLOGICAL & PHARMACEUTICAL BULLETIN, 2021, 44 (10) : 1419 - 1426
  • [25] INTERACTION OF PHOSPHOLIPID VESICLES WITH PLANAR PHOSPHOLIPID BILAYERS - EFFECT OF CALCIUM AND OTHER DIVALENT IONS
    DUZGUNES, N
    OHKI, S
    BIOPHYSICAL JOURNAL, 1979, 25 (02) : A179 - A179
  • [26] Interaction of the β amyloid - Aβ(25-35) - peptide with zwitterionic and negatively charged vesicles with and without cholesterol
    Singh, Jasmeet
    Peric, Miroslav
    CHEMISTRY AND PHYSICS OF LIPIDS, 2018, 216 : 39 - 47
  • [27] Structure of Aβ(25-35) peptide in different environments
    Shanmugam, G
    Polavarapu, PL
    BIOPHYSICAL JOURNAL, 2004, 87 (01) : 622 - 630
  • [28] Spectroscopic investigation of Ginkgo biloba terpene trilactones and their interaction with amyloid peptide Aβ(25-35)
    He, Jiangtao
    Petrovic, Ana G.
    Dzyuba, Sergei V.
    Berova, Nina
    Nakanishi, Koji
    Polavarapu, Prasad L.
    SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY, 2008, 69 (04) : 1213 - 1222
  • [29] In vitro degradation of β-amyloid[25-35] peptide
    Jost, K
    Varga, J
    Penke, S
    Zarándi, M
    PROTEIN AND PEPTIDE LETTERS, 2001, 8 (06): : 423 - 428
  • [30] Transferrin neutralization of amyloid β 25-35 cytotoxicity
    Giunta, S
    Galeazzi, R
    Valli, MB
    Corder, EH
    Galeazzi, L
    CLINICA CHIMICA ACTA, 2004, 350 (1-2) : 129 - 136