Natural stereoisomeric flavonoids exhibit different disruptive effects and the mechanism of action on Aβ42 protofibril

被引：30
作者：
Zhan, Chendi [1 ]
Lao, Zenghui [1 ]
Tang, Yiming [1 ]
Qiao, Qin [2 ]
Wei, Guanghong [1 ]
机构：
[1] Fudan Univ, Dept Phys, State Key Lab Surface Phys, Key Lab Computat Phys Sci,Minist Educ, Shanghai 200438, Peoples R China
[2] Fudan Univ, Shanghai Key Lab Med Imaging Comp & Comp Assisted, Sch Basic Med Sci, Digital Med Res Ctr, Shanghai 200032, Peoples R China
来源：
CHEMICAL COMMUNICATIONS | 2021年 / 57卷 / 35期
基金：
美国国家科学基金会;
关键词：
AMYLOID-BETA; CATECHIN; EPICATECHIN; INHIBITION; OLIGOMERS; PEPTIDE;
D O I：
10.1039/d1cc00404b
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Our simulations reveal that two enantiomeric catechins display a better disruptive effect on A beta(42) protofibril than their stereoisomer epicatechin. Unexpectedly, we find that catechins adopt both collapsed and extended states, while epicatechin populates only an extended state. Their different protofibril-disruptive effects are mostly attributed to the steric effect caused by the conformational differences.
引用
收藏
页码：4267 / 4270
页数：4
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共 25 条
  • [1] Structural conversion of neurotoxic amyloid-β1-42 oligomers to fibrils
    Ahmed, Mahiuddin
    Davis, Judianne
    Aucoin, Darryl
    Sato, Takeshi
    Ahuja, Shivani
    Aimoto, Saburo
    Elliott, James I.
    Van Nostrand, William E.
    Smith, Steven O.
    [J]. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2010, 17 (05) : 561 - U56
  • [2] Vescalagin and castalagin reduce the toxicity of amyloid-beta42 oligomers through the remodelling of its secondary structure
    Araujo, Ana R.
    Camero, Sergio
    Taboada, Pablo
    Reis, Rui L.
    Pires, Ricardo A.
    [J]. CHEMICAL COMMUNICATIONS, 2020, 56 (21) : 3187 - 3190
  • [3] Catechin and epicatechin from Smilacis chinae rhizome protect cultured rat cortical neurons against amyloid β protein (25-35)-induced neurotoxicity through inhibition of cytosolic calcium elevation
    Ban, Ju Yeon
    Jeon, So-Young
    Bae, KiWhan
    Song, Kyung-Sik
    Seong, Yeon Hee
    [J]. LIFE SCIENCES, 2006, 79 (24) : 2251 - 2259
  • [4] Chiral supramolecular coordination cages as high-performance inhibitors against amyloid-β aggregation
    Bao, Ling-Yu
    Hao, Si-Jia
    Xi, Sai-Fei
    Yan, Xiaodong
    Zhang, Hai-Xia
    Shen, Rui
    Gu, Zhi-Guo
    [J]. CHEMICAL COMMUNICATIONS, 2018, 54 (63) : 8725 - 8728
  • [5] Neuroprotective effects of green and black teas and their catechin gallate esters against β-amyloid-induced toxicity
    Bastianetto, S
    Yao, ZX
    Papadopoulos, V
    Quirion, R
    [J]. EUROPEAN JOURNAL OF NEUROSCIENCE, 2006, 23 (01) : 55 - 64
  • [6] Gantenerumab: A Novel Human Anti-Aβ Antibody Demonstrates Sustained Cerebral Amyloid-β Binding and Elicits Cell-Mediated Removal of Human Amyloid-β
    Bohrmann, Bernd
    Baumann, Karlheinz
    Benz, Joerg
    Gerber, Francoise
    Huber, Walter
    Knoflach, Frederic
    Messer, Juerg
    Oroszlan, Krisztina
    Rauchenberger, Robert
    Richter, Wolfgang F.
    Rothe, Christine
    Urban, Margit
    Bardroff, Michael
    Winter, Michael
    Nordstedt, Christer
    Loetscher, Hansruedi
    [J]. JOURNAL OF ALZHEIMERS DISEASE, 2012, 28 (01) : 49 - 69
  • [7] Antioxidant effects of Epicatechin on the hippocampal toxicity caused by Amyloid-beta 25-35 in rats
    Cuevas, Elvis
    Limon, Daniel
    Perez-Severiano, Francisca
    Diaz, Alfonso
    Ortega, Laura
    Zenteno, Edgar
    Guevara, Jorge
    [J]. EUROPEAN JOURNAL OF PHARMACOLOGY, 2009, 616 (1-3) : 122 - 127
  • [8] Quantitative analysis of flavan-3-ols in Spanish foodstuffs and beverages
    de Pascual-Teresa, S
    Santos-Buelga, C
    Rivas-Gonzalo, JC
    [J]. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2000, 48 (11) : 5331 - 5337
  • [9] Inhibition of protein misfolding and aggregation by natural phenolic compounds
    Dhouafli, Zohra
    Cuanalo-Contreras, Karina
    Hayouni, El Akrem
    Mays, Charles E.
    Soto, Claudio
    Moreno-Gonzalez, Ines
    [J]. CELLULAR AND MOLECULAR LIFE SCIENCES, 2018, 75 (19) : 3521 - 3538
  • [10] Inhibition of protein aggregation and amyloid formation by small molecules
    Doig, Andrew J.
    Derreumaux, Philippe
    [J]. CURRENT OPINION IN STRUCTURAL BIOLOGY, 2015, 30 : 50 - 56
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