Structural and mechanistic insights into amyloid‐β and α‐synuclein fibril formation and polyphenol inhibitor efficacy in phospholipid bilayers

FEBS Journal ◽  
2021 ◽  
Author(s):  
Henry M. Sanders ◽  
Blagojce Jovcevski ◽  
Michael T. Marty ◽  
Tara L. Pukala
Keyword(s):  
Amyloid Β ◽  
Fibril Formation ◽  
Phospholipid Bilayers

525 Acetylcholinesterase promotes Alzheimer's amyloid-β fibril formation

1996 ◽  
Vol 17 (4) ◽  
pp. S131
Author(s):  
N.C. Inestrosa ◽  
A. Alvarez
Keyword(s):  
Amyloid Β ◽  
Fibril Formation

scholarly journals New Class of Inhibitors of Amyloid-β Fibril Formation

2002 ◽  
Vol 277 (45) ◽  
pp. 42881-42890 ◽  
Author(s):  
Hilal A. Lashuel ◽  
Dean M. Hartley ◽  
David Balakhaneh ◽  
Aneel Aggarwal ◽  
Saul Teichberg ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Fibril Formation ◽  
New Class

Sodium-salt adduct fullerenes prevent self-association and amyloid β fibril formation: molecular dynamics approach

2020 ◽  
Vol 18 (2-3) ◽  
pp. 335-347
Author(s):  
Miguel Angel Balderas Altamirano ◽  
Gustavo Basurto-Islas ◽  
Melchor Martínez-Herrera ◽  
Juan Luis Pichardo Molina ◽  
Susana Figueroa-Gerstenmaier
Keyword(s):  
Molecular Dynamics ◽  
Sodium Salt ◽  
Amyloid Β ◽  
Fibril Formation ◽  
Self Association

A sulfated proteoglycan aggregation factor mediates amyloid-β peptide fibril formation and neurotoxicity

Amyloid ◽  
1999 ◽  
Vol 6 (4) ◽  
pp. 233-243 ◽  
Author(s):  
Joanne McLaurin ◽  
Trudy Franklin ◽  
William J Kuhns ◽  
Paul E. Fraser
Keyword(s):  
Amyloid Β ◽  
Fibril Formation ◽  
Amyloid Β Peptide ◽  
Aggregation Factor

scholarly journals Propofol and Thiopental Suppress Amyloid Fibril Formation and GM1 Ganglioside Expression through the γ-Aminobutyric Acid A Receptor

2013 ◽  
Vol 118 (6) ◽  
pp. 1408-1416 ◽  
Author(s):  
Naoki Yamamoto ◽  
Hajime Arima ◽  
Takeshi Sugiura ◽  
Hiroyuki Hirate ◽  
Hideo Taniura ◽  
...  
Keyword(s):  
Alzheimer Disease ◽  
Cell Surface ◽  
Specific Binding ◽  
Amyloid Β ◽  
Neuronal Cell ◽  
Fibril Formation ◽  
Aminobutyric Acid ◽  
Amyloid Β Protein ◽  
Gm1 Ganglioside ◽  
Free System

Abstract Background: The incidence of Alzheimer disease may increase after surgical interventions. Amyloid β-protein (Aβ) fibrillogenesis, which is closely related to Alzheimer disease, is reportedly accelerated by exposure to anesthetics. However, the effects of GM1 ganglioside (GM1) on Αβ fibrillogenesis have not yet been reported. The current study was designed to examine whether the anesthetics propofol and thiopental are associated with Αβ assembly and GM1 expression on the neuronal cell surface. Methods: PC12N cells and cultured neuronal cells were treated with propofol or thiopental, and GM1 expression in treated and untreated cells was determined by the specific binding of horseradish peroxidase-conjugated cholera toxin subunit B (n = 5). The effects of an inhibitor of the γ-aminobutyric acid A receptor was also examined (n= 5). In addition, the effects of the anesthetics on GM1 liposome-induced Αβ assembly were investigated (n = 5). Finally, the neurotoxicity of the assembled Αβ fibrils was studied by the lactate dehydrogenase release assay (n = 6). Results: Propofol (31.2±4.7%) and thiopental (34.6±10.5%) decreased GM1 expression on the cell surface through the γ-aminobutyric acid A receptor. The anesthetics inhibited Αβ fibril formation from soluble Αβ in cultured neurons. Moreover, propofol and thiopental suppressed GM1-induced fibril formation in a cell-free system (propofol, 75.8±1.9%; thiopental, 83.6±1.9%) and reduced the neurotoxicity of a mixture containing Aβ and GM1 liposomes (propofol, 35.3±16.4%; thiopental, 21.3±11.6%). Conclusions: Propofol and thiopental have direct and indirect inhibitory effects on Αβ fibrillogenesis.

Sign in / Sign up

Export Citation Format

Share Document