A method for evaluating the level of soluble β-amyloid(1-40/1-42) in Alzheimer's disease based on the binding of gelsolin to β-amyloid peptides

Abstract

In the present work, a new electrochemical strategy for the sensitive and specific detection of soluble β-amyloid Aβ(1-40/1-42) peptides in a rat model of Alzheimer's disease (AD) is described. In contrast to previous antibody-based methods, β-amyloid(1-40/1-42) was quantified based on its binding to gelsolin, a secretory protein present in the cerebrospinal fluid (CSF) and plasma. The level of soluble β-amyloid peptides in the CSF and various brain regions were found with this method to be lower in rats with AD than in normal rats. Amyloid assay: A selective gelsolin-based electrochemical probe was designed that can specifically bind the β-amyloid peptides Aβ(1-40/1-42) (yellow and green) to quantify variations in Aβ levels in Alzheimer's disease (AD). This sensitive method makes use of the amplifying features of AuNPs and was successfully used to evaluate variations in the Aβ content of the cerebrospinal fluid and brain tissues of normal and AD-affected rats.