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

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 Erratum: Characterizing affinity epitopes between prion protein and β-amyloid using an epitope mapping immunoassay

2014 ◽  
Vol 46 (5) ◽  
pp. e96-e96
Author(s):  
Mino Kang ◽  
Su Yeon Kim ◽  
Seong Soo A An ◽  
Young Ran Ju
Keyword(s):  
Prion Protein ◽  
Epitope Mapping ◽  
Β Amyloid

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 Breaking the Code of Amyloid-βOligomers

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Sylvain E. Lesné
Keyword(s):  
Prion Protein ◽  
Neurodegenerative Disorders ◽  
Biological Activities ◽  
Prion Diseases ◽  
Amyloid Proteins ◽  
Biophysical Properties ◽  
Respective Role ◽  
Amyloid Oligomers ◽  
Multiple Conformations ◽  
Frontotemporal Dementias

Departing from the original postulates that defined various neurodegenerative disorders, accumulating evidence supports a major role for soluble forms of amyloid proteins as initiator toxins in Alzheimer’s disease, Parkinson’s disease, frontotemporal dementias, and prion diseases. Soluble multimeric assemblies of amyloid-β, tau,α-synuclein, and the prion protein are generally englobed under the term oligomers. Due to their biophysical properties, soluble amyloid oligomers can adopt multiple conformations and sizes that potentially confer differential biological activities. Therein lies the problem: with sporadic knowledge and limited tools to identify, characterize, and study amyloid oligomers, how can we solve the enigma of their respective role(s) in the pathogenesis of neurodegenerative disorders? To further our understanding of these devastating diseases, the code of the amyloid oligomers must be broken.

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