Amyloid

diagnosis of AD. In vitro studies have shown that florbetapir binds selectively and saturably to β-amyloid plaques in brain tissues via the β-amyloid ligand. Once bound florbetapir allows for the density of the plaques to be measured. Florbetapir half life (T1/2 = 109.75) is significantly longer than that of C-PIB thus leading to a longer duration of action in the brain and increased accumulation in β-amyloid plaques. Ninety minutes after administration the radioactivity remaining in the blood (approximately

characterize Alzheimer’s as the accumulation of neurofibrillary tangles and amyloid plaques in the brain” (Fernandez-Enright). Amyloid plaque is the “sticky buildup” of proteins normally found in the body that divide and create “beta amyloid which is toxic to neurons in the brain” (Myers). Amyloid plaques have “different rates of growth throughout neocortical and hippocampal regions” and are formed from the “oligomers of amyloid in the intracellular and extracellular space,” and when the oligomers accumulate

There has been much research over the last 30 years on the amyloid cascade hypothesis leading to substantial supporting evidence and clinical trials. A phase I and II study has shown that the inhibition of gamma secretase by semagacestat had caused a reduction in beta amyloid synthesis in patients with mild to moderate Alzheimer’s disease (Doody et al. 2013). Gamma secretase is a protease complex involved in the processing of amyloid precursor protein. Unfortunately, a phase III trial using semagacestat

1998; Chartier-Harlin et al., 1994; Corder et al., 1993). AD is strongly associated with two types of pathologies, amyloid-β plaque and the phosphorylated tau proteins that can often lead to neurofibrillary tangles (NFTs) (Kim et al., 2009). The three alleles of ApoE (E2, E3, and E4) have been found to show dosage-dependent effects that negatively affects the clearance of amyloid-β plaque, with E4 showing the least clearance whereas E2 showing the most (Deane et al., 2008; Holtzman, 2004). Additionally

focus on the investigation of viral infections involved in neurodegenerative diseases. Data suggests that viral infections promote hallmark events seen in neuronal degeneration such as in Alzheimer's Disease (AD). In AD, protein aggregates of β-amyloid peptides forming plaques and neurofibrillary tangles composed of hyperphosphorylated tau has been shown to impair brain functions. Areas affected are the hippocampus and cerebral cortex responsible for cognitive and locomotor skills. Other contributing

with two major pathologies, the accumulation of amyloid-B and tau phosphorylation (_). These pathologies have long been implicated with the gene Alipoprotein E (ApoE) which continually showed a dosage-dependent effect on amyloid-B clearance (_). Many studies have shown correlated linkage between ApoE and tau as well as their possible interactions (_). Tau phosphorylation has continually been found among many AD patients suffering with and without amyloid-B deposition (_). However, it is still unclear

impacted by microglia and astroglia. 3 The microglia are distributed evenly across the brain and are activated by protein aggregation and neuronal cell death. 3 Specifically related to AD, the two chief proteins involved are amyloid-B and tau.3 An accumulation of microglia around amyloid-B plaques has been documented in post-mortem human brains and in animal models with AD.3 Research has yet to clearly determine if microglial activation plays a beneficial or detrimental role in the progression of AD..3

The misfolding proteins can lead to many different diseases for human bodies. So, it’s important to prevent or disrupt the pathways to a misfolded protein. To do so, we first need to understand the function of protein folding, amyloid fibril as well as alpha helix, beta sheets, Aβ , and α-Synuclein…how they affected the structures of each protein in certain diseases. Then, it would be a good fundamental tool that may lead to the development for treating diseases. However, the challenge

tangles and senile plaques. (4) These are commonly known as plaques and tangles and are caused by the build-up of two proteins. The plaques are a build-up of the protein beta-amyloid (β-amyloid) while the tangles are formed by the build-up of the protein tau, even though both are found in Alzheimer's disease only the β-amyloid plaques are unique to the disease and it is these plaques that are believed to be the primary cause of Alzheimer's.

of senile plaques composed of beta-amyloid proteins can cause blockage of neuron signaling at the synapses [2]. Tau proteins, which are microtubule associated, are naturally found in the brain and take part in the nutrient transport network in the brain. The degeneration of Tau proteins creates congregates and forms Neuron Fiber Tangles, which is hypothesized to correlate with brain necrosis and brain size [1]. The detection of biomarkers specifically beta-amyloid peptides and Tau proteins could allow