scholarly journals Time-Dependent Lipid Dynamics, Organization and Peptide-Lipid Interaction in Phospholipid Bilayers with Incorporated β-Amyloid Oligomers

2020 ◽  
Vol 11 (19) ◽  
pp. 8329-8336
Author(s):  
Wei Qiang ◽  
Katelynne E. Doherty ◽  
Lukas M. Klees ◽  
Yuto Tobin-Miyaji
Keyword(s):  
Phospholipid Bilayers ◽  
Time Dependent ◽  
Lipid Dynamics ◽  
Amyloid Oligomers ◽  
Β Amyloid ◽  
Lipid Interaction

scholarly journals Cell stiffness and ROS level alterations in living neurons mediated by β-amyloid oligomers measured by scanning ion-conductance microscopy.

2021 ◽  
Vol 27 (S1) ◽  
pp. 500-502
Author(s):  
Oleg Suchalko ◽  
Roman Timoshenko ◽  
Alexander Vaneev ◽  
Vasilii Kolmogorov ◽  
Nikita Savin ◽  
...  
Keyword(s):  
Cell Stiffness ◽  
Ion Conductance ◽  
Scanning Ion Conductance Microscopy ◽  
Amyloid Oligomers ◽  
Β Amyloid ◽  
Living Neurons

scholarly journals Local and Use-Dependent Effects of β-Amyloid Oligomers on NMDA Receptor Function Revealed by Optical Quantal Analysis

2016 ◽  
Vol 36 (45) ◽  
pp. 11532-11543 ◽  
Author(s):  
Brooke L. Sinnen ◽  
Aaron B. Bowen ◽  
Emily S. Gibson ◽  
Matthew J. Kennedy
Keyword(s):  
Nmda Receptor ◽  
Receptor Function ◽  
Amyloid Oligomers ◽  
Quantal Analysis ◽  
Nmda Receptor Function ◽  
Β Amyloid

scholarly journals ROSETTA-informed design of structurally stabilized cyclic anti-amyloid peptides

2019 ◽  
Vol 32 (2) ◽  
pp. 47-57 ◽  
Author(s):  
Chandler B Est ◽  
Parth Mangrolia ◽  
Regina M Murphy
Keyword(s):  
Amyloid Fibril ◽  
Cyclic Peptide ◽  
Bond Formation ◽  
Amyloid Peptides ◽  
Linear Peptide ◽  
Toxic Species ◽  
Disulfide Linkages ◽  
Amyloid Oligomers ◽  
Β Amyloid ◽  
Β Sheet

Abstract β-amyloid oligomers are thought to be the most toxic species formed en route to fibril deposition in Alzheimer’s disease. Transthyretin is a natural sequestering agent of β-amyloid oligomers: the binding site to β-amyloid has been traced to strands G/H of the inner β-sheet of transthyretin. A linear peptide, with the same primary sequence as the β-amyloid binding domain on transthyretin, was moderately effective at inhibiting β-amyloid fibril growth. Insertion of a β-turn template and cyclization greatly increased stability against proteolysis and improved efficacy as an amyloid inhibitor. However, the cyclic peptide still contained a significant amount of disorder. Using the Simple Cyclic Peptide Application within ROSETTA as an in silico predictor of cyclic peptide conformation and stability, we investigated putative structural enhancements, including stabilization by disulfide linkages and insertion of a second β-turn template. Several candidates were synthesized and tested for secondary structure and ability to inhibit β-amyloid aggregation. The results demonstrate that cyclization, β-sheet structure and conformational homogeneity are all preferable design features, whereas disulfide bond formation across the two β-strands is not preferable.

scholarly journals A Foldamer-Dendrimer Conjugate Neutralizes Synaptotoxic β-Amyloid Oligomers

PLoS ONE ◽  
2012 ◽  
Vol 7 (7) ◽  
pp. e39485 ◽  
Author(s):  
Lívia Fülöp ◽  
István M. Mándity ◽  
Gábor Juhász ◽  
Viktor Szegedi ◽  
Anasztázia Hetényi ◽  
...  
Keyword(s):  
Amyloid Oligomers ◽  
Β Amyloid

scholarly journals Size-dependent neurotoxicity of β-amyloid oligomers

2010 ◽  
Vol 496 (2) ◽  
pp. 84-92 ◽  
Author(s):  
Paulius Cizas ◽  
Rima Budvytyte ◽  
Ramune Morkuniene ◽  
Radu Moldovan ◽  
Matteo Broccio ◽  
...  
Keyword(s):  
Size Dependent ◽  
Amyloid Oligomers ◽  
Β Amyloid

scholarly journals What Does Time-Dependent Fluorescence Shift (TDFS) in Biomembranes (and Proteins) Report on?

2021 ◽  
Vol 9 ◽  
Author(s):  
Federica Scollo ◽  
Hüseyin Evci ◽  
Mariana Amaro ◽  
Piotr Jurkiewicz ◽  
Jan Sykora ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Nmr Spectroscopy ◽  
Experimental Method ◽  
Phospholipid Bilayers ◽  
Time Dependent ◽  
Interfacial Region ◽  
Oxidized Phospholipids ◽  
Degree Of Hydration ◽  
Fluorescence Dye ◽  
Dynamics Simulations

The organization of biomolecules and bioassemblies is highly governed by the nature and extent of their interactions with water. These interactions are of high intricacy and a broad range of methods based on various principles have been introduced to characterize them. As these methods view the hydration phenomena differently (e.g., in terms of time and length scales), a detailed insight in each particular technique is to promote the overall understanding of the stunning “hydration world.” In this prospective mini-review we therefore critically examine time-dependent fluorescence shift (TDFS)—an experimental method with a high potential for studying the hydration in the biological systems. We demonstrate that TDFS is very useful especially for phospholipid bilayers for mapping the interfacial region formed by the hydrated lipid headgroups. TDFS, when properly applied, reports on the degree of hydration and mobility of the hydrated phospholipid segments in the close vicinity of the fluorophore embedded in the bilayer. Here, the interpretation of the recorded TDFS parameters are thoroughly discussed, also in the context of the findings obtained by other experimental techniques addressing the hydration phenomena (e.g., molecular dynamics simulations, NMR spectroscopy, scattering techniques, etc.). The differences in the interpretations of TDFS outputs between phospholipid biomembranes and proteins are also addressed. Additionally, prerequisites for the successful TDFS application are presented (i.e., the proper choice of fluorescence dye for TDFS studies, and TDFS instrumentation). Finally, the effects of ions and oxidized phospholipids on the bilayer organization and headgroup packing viewed from TDFS perspective are presented as application examples.

S4-03-03: Direct neuron to neuron transmission of β-amyloid oligomers causes neurodegeneration

2011 ◽  
Vol 7 ◽  
pp. e2-e2
Author(s):  
Sangeeta Nath ◽  
Lotta Agholme ◽  
Firoz Roshan Kurudenkandy ◽  
Björn Granseth ◽  
Jan Marcusson ◽  
...  
Keyword(s):  
Amyloid Oligomers ◽  
Β Amyloid

Membrane‐bound β‐amyloid oligomers are recruited into lipid rafts by a fyn‐dependent mechanism

2007 ◽  
Vol 22 (5) ◽  
pp. 1552-1559 ◽  
Author(s):  
Ritchie Williamson ◽  
Alessia Usardi ◽  
Diane P. Hanger ◽  
Brian H. Anderton
Keyword(s):  
Lipid Rafts ◽  
Amyloid Oligomers ◽  
Membrane Bound ◽  
Β Amyloid ◽  
Dependent Mechanism

scholarly journals β-amyloid oligomers and prion protein

Prion ◽  
2011 ◽  
Vol 5 (1) ◽  
pp. 10-15 ◽  
Author(s):  
Gianluigi Forloni ◽  
Claudia Balducci
Keyword(s):  
Prion Protein ◽  
Amyloid Oligomers ◽  
Β Amyloid
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