Amyloid beta peptide (Aβ) is produced through the proteolytic processing of a transmembrane protein, amyloid precursor protein (APP), by β- and γ-secretases. Aβ accumulation in the brain is proposed to be an early toxic event in the pathogenesis of Alzheimer's disease, which is the most common form of dementia associated with plaques and tangles in the brain. Currently, it is unclear what the physiological and pathological forms of Aβ are and by what mechanism Aβ causes dementia. Moreover, there are no efficient drugs to stop or reverse the progression of Alzheimer's disease. In this paper, we review the structures, biological functions, and neurotoxicity role of Aβ. We also discuss the potential receptors that interact with Aβ and mediate Aβ intake, clearance, and metabolism. Additionally, we summarize the therapeutic developments and recent advances of different strategies for treating Alzheimer's disease. Finally, we will report on the progress in searching for novel, potentially effective agents as well as selected promising strategies for the treatment of Alzheimer's disease. These prospects include agents acting on Aβ, its receptors and tau protein, such as small molecules, vaccines and antibodies against Aβ; inhibitors or modulators of β- and γ-secretase; Aβ-degrading proteases; tau protein inhibitors and vaccines; amyloid dyes and microRNAs.

/pdf/amyloid-beta-structure-biology-and-structure-based-3y96h59gd4.pdf

Amyloid beta: structure, biology and structure-based therapeutic development

http://www.austinblanco.com/Resources/Koronyo-Hamaoui_Maya_Neuroimage_2010.pdf

Identification of amyloid plaques in retinas from Alzheimer's patients and noninvasive in vivo optical imaging of retinal plaques in a mouse model

Imaging modalities such as microcomputed tomography (micro-CT), micropositron emission tomography (micro-PET), high-resolution magnetic resonance imaging (MRI), optical imaging, and high-resolution ultrasound have become invaluable tools in preclinical pharmaceutical research. They are used to noninvasively investigate, under in vivo conditions, the rodent biology and metabolism, the disease models, and the pharmacokinetics/pharmacodynamics of drugs. Since the advantages and limitations of each approach determine its application, a small animal imaging laboratory in a pharmaceutical environment should ideally provide access to several techniques. In this chapter we illustrate how these imaging techniques may be used to obtain relevant information for the phenotyping of transgenic mice and for the analysis of compounds in murine models of disease, using Alzheimer’s disease as an example.

https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/pdf/10.1002/nbm.1153

In Vivo Mouse Imaging and Spectroscopy in Drug Discovery

Longitudinal PET-MRI study on the dynamics of β-amyloid deposition and regional cerebral blood flow in the Alzheimer's disease mouse brain.

Longitudinal PET-MRI reveals [beta]-amyloid deposition and rCBF dynamics and connects vascular amyloidosis to quantitative loss of perfusion

In vivo imaging and quantification of amyloid-β plaque (Aβ) burden in small-animal models of Alzheimer's disease (AD) is a valuable tool for translational research such as developing specific imaging markers and monitoring new therapy approaches. Methodological constraints such as image resolution of positron emission tomography (PET) and lack of suitable AD models have limited the feasibility of PET in mice. In this study, we evaluated a feasible protocol for PET imaging of Aβ in mouse brain with [11C]PiB and specific activities commonly used in human studies. In vivo mouse brain MRI for anatomical reference was acquired with a clinical 1.5 T system. A recently characterized APP/PS1 mouse was employed to measure Aβ at different disease stages in homozygous and hemizygous animals. We performed multi-modal cross-validations for the PET results with ex vivo and in vitro methodologies, including regional brain biodistribution, multi-label digital autoradiography, protein quantification with ELISA, fluorescence microscopy, semi-automated histological quantification and radioligand binding assays. Specific [11C]PiB uptake in individual brain regions with Aβ deposition was demonstrated and validated in all animals of the study cohort including homozygous AD animals as young as nine months. Corresponding to the extent of Aβ pathology, old homozygous AD animals (21 months) showed the highest uptake followed by old hemizygous (23 months) and young homozygous mice (9 months). In all AD age groups the cerebellum was shown to be suitable as an intracerebral reference region. PET results were cross-validated and consistent with all applied ex vivo and in vitro methodologies. The results confirm that the experimental setup for non-invasive [11C]PiB imaging of Aβ in the APP/PS1 mice provides a feasible, reproducible and robust protocol for small-animal Aβ imaging. It allows longitudinal imaging studies with follow-up periods of approximately one and a half years and provides a foundation for translational Alzheimer neuroimaging in transgenic mice.

/pdf/small-animal-pet-imaging-of-amyloid-beta-plaques-with-11c-3pf7rndnm1.pdf

Small-Animal PET Imaging of Amyloid-Beta Plaques with [11C]PiB and Its Multi-Modal Validation in an APP/PS1 Mouse Model of Alzheimer's Disease

Purpose
The purpose of this study was to evaluate the capacity of [11C]6-OH-BTA-1 and positron emission tomography (PET) to quantify β-amyloid (Aβ) plaques in the Tg2576 mouse model of Alzheimer’s disease (AD).

PET imaging of brain with the β-amyloid probe, [11C]6-OH-BTA-1, in a transgenic mouse model of Alzheimer’s disease

PET imaging of transgenic mice TG2576 using the beta-amyloid radioligand, [C-11]PIB

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PET imaging of brain with the β-amyloid probe, [11C]6-OH-BTA-1, in a transgenic mouse model of Alzheimer’s disease

PET imaging of transgenic mice TG2576 using the beta-amyloid radioligand, [C-11]PIB