Tau protein belongs to a class of microtubule-binding proteins (MAP) which all originate from the common MAPT gene located on chromosome [1,2]. Tau proteins are primarily found in neurons, where they interact with microtubules and serve to stabilize microtubules in neural axons. The malfunction of tau is one of the major causes of Alzheimer's Disease (AD), however, the early detection and treatment of AD are still elusive. The detection of tau species and their levels was achieved through the use of electrochemical immunoassay based on anti-tau antibodies immobilized on a gold surface for potential use in real-time detection of tau as a biomarker for AD.  The anti-tau antibodies were bound to a carboxylic acid-modified gold surface, and EIS was used to characterize the affinity of antibody for various forms of tau: non-phosphorylated, phosphorylated and aggregated tau.  The modulation in the electrochemical signal was due to antibody binding to tau with high specificity and selectivity. The electrochemical immunosensor did not respond to other protein, such as bovine serum albumin.  The electroimmunosensor was tested in cell lysate to determine the utility of electrochemical platform in biological system and compared to the ELISA methodology.   1.               Mandelkow, EM, Mandelkow E. Biochemistry and cell biology of tau protein in neurofibrillary degeneration, Cold Spring Harb Perspect Med. 2012, 2, a006247. 2.               Billingsley, ML., Kincaid, RL. Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration. Biochem J. 1997, 323, 577-91.

Detection of tau biomarkers using tau specific antibodies immobilized on a gold surface

248th National Meeting (2014)

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