Characterizing Protein-Protein Interactions in Alzheimer's Disease Using the ProteOn™ XPR36 System

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Learn how Alzheimer's researchers at Boston University use the ProteOn XPRs6 system to characterize the protein-protein interactions that are the hallmark of this disease. Their findings could lead to a new class of therapeutic drugs for Alzheimer's treatment.

The progressive dementia seen in Alzheimer's disease is associated with an accumulation in the brain of the amyloid-β (Aβ) peptide, a cleavage product of the amyloid precursor protein. Compelling evidence suggests that soluble, oligomeric assemblies of Aβ are primarily responsible for the synaptic dysfunction underlying the cognitive decline in Alzheimer's disease. Recently, the cellular prion protein has emerged as a novel and unexpected candidate receptor for Aβ oligomers.

Utilizing several in vitro assays, Emiliano Biasini and colleagues showed that a soluble, proteolytic fragment of the prion protein, called N1, binds to a precise assembly of Aβ oligomers with nanomolar affinity. They also discovered that N1 inhibits the polymerization of Aβ oligomers into amyloid fibrils, and suppress their neurotoxic effects in vitro and in vivo. Collectively, these data provide strong experimental evidence supporting the idea that N1, or small peptides derived from it, could be potent inhibitors of Aβ oligomer toxicity and represent an entirely new class of therapeutic agents for Alzheimer's disease.

The ProteOn XPR36 system enables high-throughput multiplexed protein-protein assays, improving efficiency and reducing the time and cost of experiments, which accelerates the pace of disease research.

Presenter:
Emiliano Biasini, PhD
Dept. of Biochemistry
Boston University School of Medicine

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