Alzheimer's Disease Abstract

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Abstract Every 67 seconds someone in the United States develops Alzheimer's disease (AD). AD is a neurodegenerative condition characterized by cognitive decline accompanied by memory loss. It is the only top ten cause of death in the United States which cannot be prevented, cured, or slowed. One of the proposed causes of AD is the formation of structures containing amyloid fibrils. Amyloid fibrils are insoluble fibrous protein aggregates sharing specific structural traits. Aside from AD, amyloid fibrils are associated with twenty other known human diseases, which arise from eighteen naturally occurring proteins or polypeptides which improperly fold to cause disease. Most of the current detection methods for AD are post-symptomatic. This means …show more content…

According to the Mayo Clinic, tangles are formed by interwoven tau proteins and plaques are formed by clusters of beta-amyloid proteins. Much research is focused on the beta-amyloid peptide, which forms amyloid fibrils and plaques. Amyloid fibrils are insoluble fibrous protein aggregates sharing specific structural traits. Aside from AD, amyloid fibrils are associated with over twenty other known human diseases, which arise from eighteen naturally occurring proteins or polypeptides which improperly fold to cause disease. The timeline of amyloid fibril formation consists of three distinct phases: the lag time phase, the elongation phase, and the asymptotic phase. During the lag time, proteins are beginning to form toxic species, but the concentration is difficult to measure. During the elongation phase, the detectable fibrils elongate exponentially. And finally, during the asymptotic phase, most of the available protein has been converted to amyloid fibrils; therefore, the growth discontinues, and the concentration remains …show more content…

Amyloid fibrils are toxic protein structures characterized by the presence of densely stacked β-sheets. Amyloid protein can arise from eighteen naturally occurring proteins or polypeptides which improperly fold to cause disease via a process called amyloidgenesis (Ramirez-Alvarado, 2000). These structures are extremely strong and appear to be immune to the effects of denaturing agents and proteases. The body’s inability to deconstruct these fibrous proteins leads to amyloidosis, or the abnormal accumulation of amyloid aggregates in the tissues of the body. The progression of this condition can lead to the manifestation of different pathogenic species, including the plaques and tangles which have long been associated with Alzheimer’s disease (Mayo Clinic,

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