scholarly journals Targeting Soluble Amyloid Oligomers in Alzheimer's Disease through Disordered Prion Peptides

2019 ◽  
Vol 116 (3) ◽  
pp. 495a
Author(s):  
Zachary A. Levine
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Oligomers

P2-392: The efficacy of anti-beta-amyloid oligomers antibody in mouse models of Alzheimer's disease

2013 ◽  
Vol 9 ◽  
pp. P502-P502
Author(s):  
Yasuhide Okamoto ◽  
Tatsuki Yokoseki ◽  
Takamatsu Naofumi ◽  
Yukiho Imai ◽  
Shinobu Fujii
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Mouse Models ◽  
Beta Amyloid ◽  
Amyloid Oligomers

scholarly journals Amyloid and Alzheimer's Disease: Inside and Out

2012 ◽  
Vol 39 (3) ◽  
pp. 286-298 ◽  
Author(s):  
Joshua H. K. Tam ◽  
Stephen H. Pasternak
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Clinical Trials ◽  
Clinical Implications ◽  
Amyloid Cascade Hypothesis ◽  
Amyloid Peptides ◽  
Amyloid Hypothesis ◽  
Lysosomal Dysfunction ◽  
Amyloid Oligomers ◽  
Amyloid Cascade

Alzheimer's disease (AD) is poised to become the most serious healthcare issue of our generation. The leading theory of AD pathophysiology is the Amyloid Cascade Hypothesis, and clinical trials are now proceeding based on this hypothesis. Here, we review the original evidence for the Amyloid Hypothesis, which was originally focused on the extracellular deposition of beta amyloid peptides (Aβ) in large fibrillar aggregates, as well as how this theory has been extended in recent years to focus on highly toxic small soluble amyloid oligomers. We will also examine emerging evidence that Aβ may actually begin to accumulate intracellularly in lysosomes, and the role for intracellular Aβ and lysosomal dysfunction may play in AD pathophysiology. Finally, we will review the clinical implications of these findings.

scholarly journals Development of a quantitative and conformation-sensitive ATR-FTIR biosensor for Alzheimer's disease: The effect of deuteration on the detection of the Aβ peptide

2010 ◽  
Vol 24 (1-2) ◽  
pp. 61-66 ◽  
Author(s):  
Emilie Kleiren ◽  
Jean-Marie Ruysschaert ◽  
Erik Goormaghtigh ◽  
Vincent Raussens
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Early Stage ◽  
Amyloid Β ◽  
Attenuated Total Reflection ◽  
Aβ Peptide ◽  
Deuterated Water ◽  
Germanium Crystal ◽  
Amyloid Oligomers ◽  
New Type

Alzheimer's disease (AD) is the most common form of dementia worldwide and represents a growing socio-economical issue. To date, no reliable diagnosis can be obtained at an early-stage of the disease, though it is now recognized that the aggregation of the amyloid β (Aβ) peptide is responsible for the onset of the disease. Recent studies have shown that soluble amyloid oligomers present in the physiological fluids were the most neurotoxic species and correlated best with the first signs of cognitive decline, which makes them good biomarkers in the development of a diagnostic tool.We describe here a new type of biosensor, based on attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopy, that would be able to specifically detect and quantify the presence of the different forms of the Aβ peptide in solution. The principle of the detection relies on the recognition of the peptides by specific antibodies that were previously grafted on the surface of an ATR element, consisting of a functionalized germanium crystal. We show that the BIA-ATR technology is able to detect the presence of Aβ if incubated in deuterated water and that this step is crucial in the development of our conformation-sensitive biosensor for AD.

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