scholarly journals All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers

2012 ◽  
Vol 8 (3) ◽  
pp. 1143-1152 ◽  
Author(s):  
Ricardo Capone ◽  
Hyunbum Jang ◽  
Samuel A. Kotler ◽  
Laura Connelly ◽  
Fernando Teran Arce ◽  
...  
Keyword(s):  
Ion Channels ◽  
Lipid Bilayers ◽  
Amyloid Peptide ◽  
Β Amyloid ◽  
Β Amyloid Peptide

Channel Formation in Planar Lipid Bilayers by a Neurotoxic Fragment of the β-Amyloid Peptide

1994 ◽  
Vol 202 (2) ◽  
pp. 1142-1148 ◽  
Author(s):  
T. Mirzabekov ◽  
M.C. Lin ◽  
W.L. Yuan ◽  
P.J. Marshall ◽  
M. Carman ◽  
...  
Keyword(s):  
Lipid Bilayers ◽  
Amyloid Peptide ◽  
Planar Lipid Bilayers ◽  
Channel Formation ◽  
Β Amyloid ◽  
Β Amyloid Peptide

scholarly journals Choline Modulation of the Aβ P1-40 Channel Reconstituted into a Model Lipid Membrane

2010 ◽  
Vol 2010 ◽  
pp. 1-12
Author(s):  
Daniela Meleleo ◽  
Gabriella Notarachille ◽  
Silvia Micelli
Keyword(s):  
Lipid Bilayers ◽  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Lipid Membrane ◽  
Cd Spectroscopy ◽  
Amyloid Peptide ◽  
Random Coil ◽  
Ion Conductance ◽  
Β Amyloid ◽  
Β Amyloid Peptide

Nicotinic acetylcholine receptors (AChRs), implicated in memory and learning, in subjects affected by Alzheimer's disease result altered. Stimulation of α7-nAChRs inhibits amyloid plaques and increases ACh release. β-amyloid peptide (AβP) forms ion channels in the cell and model phospholipid membranes that are retained responsible in Alzheimer disease. We tested if choline, precursor of ACh, could affect the AβP1-40 channels in oxidized cholesterol (OxCh) and in palmitoyl-oleoyl-phosphatidylcholine (POPC):Ch lipid bilayers. Choline concentrations of 5 × 10−11 M–1.5 × 10−8 M added to thecis- ortrans-side of membrane quickly increased AβP1-40 ion channel frequency (events/min) and ion conductance in OxCh membranes, but not in POPC:Ch membranes. Circular Dichroism (CD) spectroscopy shows that after 24 and 48 hours of incubation with AβP1-40, choline stabilizes the random coil conformation of the peptide, making it less prone to fibrillate. These actions seem to be specific in that ACh is ineffective either in solution or on AβP1-40 channel incorporated into PLMs.

scholarly journals Cholesterol Modulates the Interaction of β-Amyloid Peptide with Lipid Bilayers

2009 ◽  
Vol 96 (10) ◽  
pp. 4299-4307 ◽  
Author(s):  
Liming Qiu ◽  
Anthony Lewis ◽  
John Como ◽  
Mark W. Vaughn ◽  
Juyang Huang ◽  
...  
Keyword(s):  
Lipid Bilayers ◽  
Amyloid Peptide ◽  
Β Amyloid ◽  
Β Amyloid Peptide

N2L, a novel lipoic acid-niacin dimer protects HT22 cells against β-amyloid peptide-induced damage through attenuating apoptosis

2019 ◽  
Vol 34 (6) ◽  
pp. 1761-1770 ◽  
Author(s):  
Rikang Wang ◽  
Lang Zhang ◽  
Rifang Liao ◽  
Qian Li ◽  
Rongbiao Pi ◽  
...  
Keyword(s):  
Lipoic Acid ◽  
Amyloid Peptide ◽  
Ht22 Cells ◽  
Β Amyloid ◽  
Β Amyloid Peptide

scholarly journals Mutagenic analysis of the nucleation propensity of oxidized Alzheimer's β-amyloid peptide

2005 ◽  
Vol 14 (8) ◽  
pp. 2125-2131 ◽  
Author(s):  
Tony Christopeit ◽  
Peter Hortschansky ◽  
Volker Schroeckh ◽  
Karlheinz Gührs ◽  
Giorgia Zandomeneghi ◽  
...  
Keyword(s):  
Amyloid Peptide ◽  
Β Amyloid ◽  
Β Amyloid Peptide
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