Abstract
The aggregation of β-amyloid peptide (Aβ) into fibrils plays an important role in the pathogenesis of Alzheimer’s disease (AD). Metal ions including copper and zinc are closely connected to the precipitation and toxicity of Aβ. In this study, a surface plasmon resonance (SPR) biosensor was constructed to investigate the interactions between Aβ and metal ions. Aβ peptide was immobilized on the SPR chip surface through a preformed alkanethiol self-assembled monolayer (SAM). Our observations indicate that the immobilized Aβ undergoes a conformational change upon exposure to the metal ions. A difference in metal binding affinity between Aβ1–28 and Aβ1–42 was also detected. The results suggest that SPR is an effective method to characterize the interactions between Aβ and metal ions.
Highlights
Alzheimer’s disease (AD), which is characterized by irreversible and progressive neurodegeneration, is the dominant cause of dementia
The successful immobilization of the Aβ peptide on the sensor chip surface was tested by injecting a Zn2+ ion solution into the flow chamber and pumping it across the Aβ-immobilized sensing surface
To confirm that the net change is induced by the metal ions, we conducted a control experiment in which Zn2+ ions flowed over an ethanolamine-blocked surface without the immobilization of Aβ peptide
Summary
Alzheimer’s disease (AD), which is characterized by irreversible and progressive neurodegeneration, is the dominant cause of dementia. A large body of evidence suggests that metal ions such as copper, zinc and iron may induce the aggregation of Aβ peptides, and these ligands may act as seeding factors in the formation of amyloid plaques [6,7,8,9,10]. 400 μM, respectively [11] These metal ions bind at the N-terminus (amino acids 1–16) and influence aggregation behavior. Intensive efforts have been made to study the primary interaction of Aβ peptide with metal ions. A custom-built flow-injection (FI) SPR instrument equipped with a bicell detector was constructed in our lab and used to investigate the interactions between Aβ1–16 and metal ions [22]. To further test the feasibility of this biosensor, the interactions between metal ions and Aβ1–28 or the actual senile plaque component, Aβ1–42, were investigated
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