Alzheimer's disease is a neurodegenerative disorder with one of the highest prevalences. The cause of the disease is thought to be the pathological accumulation of amyloid-beta aggregates in the brain. There are several phenomena that can influence this pathological accumulation, with the enhanced levels of toxic metals being among them. Their accumulation can not only generate reactive oxygen species, accelerating the accumulation of amyloid-beta in Alzheimer's patients, but it can also interact and bind to amyloid-beta peptides. Therefore, controlling the interaction dynamics of toxic metals and amyloid-beta could help to decrease the levels of oxidative stress. Here, the researchers propose a non-toxic conjugated polymer that binds iron-containing proteins to interact with the iron present in amyloid-beta protofibril aggregates and decrease their accumulation. Cerebrospinal fluid from healthy individuals was doped with amyloid-beta 40 with and without iron to test the anti-aggregation activity of the polymer. The results show that the polymer was able to disrupt the fibril formation of amyloid-beta under physiological conditions in the cerebrospinal fluid samples, leading to less toxic forms of amyloid-beta peptides. This study brings a new tool in the treatment of Alzheimer's disease through the disruption of the pathological aggregation of amyloid beta and fibril formation.
A rapid and sensitive detection of ferritin at a nanomolar level and disruption of amyloid β fibrils using fluorescent conjugated polymer
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