scholarly journals High-resolution probing of early events in amyloid-β aggregation related to Alzheimer's disease

2020 ◽  
Vol 56 (34) ◽  
pp. 4627-4639 ◽  
Author(s):  
Bikash R. Sahoo ◽  
Sarah J. Cox ◽  
Ayyalusamy Ramamoorthy
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
High Resolution ◽  
Structure Elucidation ◽  
Amyloid Β ◽  
Atomic Resolution ◽  
High Resolution Structure ◽  
Resolution Structure

High-resolution structure elucidation of Alzheimer's amyloid-β oligomer is crucial to delineate its pathological phenotype. NMR provides atomic-resolution details of amyloid-β oligomer that could aid in the development of structure-based therapeutics.

High-Resolution Separation of Amyloid β-Peptides: Structural Variants Present in Alzheimer's Disease Amyloid

2002 ◽  
Vol 67 (1) ◽  
pp. 294-301 ◽  
Author(s):  
Jan Näslund ◽  
Anders R. Karlström ◽  
Lars O. Tjernberg ◽  
Angelika Schierhorn ◽  
Lars Terenius ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
High Resolution ◽  
Amyloid Β ◽  
Structural Variants

scholarly journals Comparing the Folds of Prions and Other Pathogenic Amyloids

Pathogens ◽  
2018 ◽  
Vol 7 (2) ◽  
pp. 50 ◽  
Author(s):  
José Flores-Fernández ◽  
Vineet Rathod ◽  
Holger Wille
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Amyloid Β ◽  
Paired Helical Filaments ◽  
X Ray ◽  
Cryo Electron Microscopy ◽  
Incompatibility System ◽  
High Resolution Structure ◽  
Jakob Disease ◽  
Resolution Structure

Pathogenic amyloids are the main feature of several neurodegenerative disorders, such as Creutzfeldt–Jakob disease, Alzheimer’s disease, and Parkinson’s disease. High resolution structures of tau paired helical filaments (PHFs), amyloid-β(1-42) (Aβ(1-42)) fibrils, and α-synuclein fibrils were recently reported using cryo-electron microscopy. A high-resolution structure for the infectious prion protein, PrPSc, is not yet available due to its insolubility and its propensity to aggregate, but cryo-electron microscopy, X-ray fiber diffraction, and other approaches have defined the overall architecture of PrPSc as a 4-rung β-solenoid. Thus, the structure of PrPSc must have a high similarity to that of the fungal prion HET-s, which is part of the fungal heterokaryon incompatibility system and contains a 2-rung β-solenoid. This review compares the structures of tau PHFs, Aβ(1-42), and α-synuclein fibrils, where the β-strands of each molecule stack on top of each other in a parallel in-register arrangement, with the β-solenoid folds of HET-s and PrPSc.

O2-02-01: HIGH RESOLUTION STRUCTURE OF AMYLOID-β(1-42) FIBRILS

2006 ◽  
Vol 14 (7S_Part_11) ◽  
pp. P610-P611
Author(s):  
Dieter Willbold ◽  
Lothar Gremer ◽  
Daniel Schölzel ◽  
Carla Schenk ◽  
Hoyer Wolfgang ◽  
...  
Keyword(s):  
High Resolution ◽  
Amyloid Β ◽  
High Resolution Structure ◽  
Resolution Structure

Amyloid β-peptide and Alzheimer's disease

2014 ◽  
Vol 56 ◽  
pp. 99-110 ◽  
Author(s):  
David Allsop ◽  
Jennifer Mayes
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Senile Plaques ◽  
Strong Support ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Amyloid Cascade Hypothesis ◽  
Sequence Of Events ◽  
Aβ Amyloid ◽  
Amyloid Cascade

One of the hallmarks of AD (Alzheimer's disease) is the formation of senile plaques in the brain, which contain fibrils composed of Aβ (amyloid β-peptide). According to the ‘amyloid cascade’ hypothesis, the aggregation of Aβ initiates a sequence of events leading to the formation of neurofibrillary tangles, neurodegeneration, and on to the main symptom of dementia. However, emphasis has now shifted away from fibrillar forms of Aβ and towards smaller and more soluble ‘oligomers’ as the main culprit in AD. The present chapter commences with a brief introduction to the disease and its current treatment, and then focuses on the formation of Aβ from the APP (amyloid precursor protein), the genetics of early-onset AD, which has provided strong support for the amyloid cascade hypothesis, and then on the development of new drugs aimed at reducing the load of cerebral Aβ, which is still the main hope for providing a more effective treatment for AD in the future.

Minimalistic Design Approach for Multi-Reactivity against Free Radicals and Metal-Free and Metal-Bound Amyloid-β Peptides: Redox-Based Substitutions of Benzene

2019 ◽  
Author(s):  
Mingeun Kim ◽  
Juhye Kang ◽  
Misun Lee ◽  
Jiyeon Han ◽  
Geewoo Nam ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Free Radicals ◽  
Amyloid Β ◽  
Design Strategy ◽  
Design Approach ◽  
Metal Free

We report a minimalistic redox-based design strategy for engineering compact molecules based on the simplest aromatic framework, benzene, with multi-reactivity against free radicals, metal-free amyloid-β, and metal-bound amyloid-β, implicated in the most common form of dementia, Alzheimer’s disease.

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