Detection of β-amyloid peptide (1–16) and amyloid precursor protein (APP770) using spectroscopic ellipsometry and QCM techniques: A step forward towards Alzheimers disease diagnostics

MUSTAFA, M. K., NABOK, A., PARKINSON, D., TOTHILL, I. E., SALAM, F. and TSARGORODSKAYA, A. (2010). Detection of β-amyloid peptide (1–16) and amyloid precursor protein (APP770) using spectroscopic ellipsometry and QCM techniques: A step forward towards Alzheimers disease diagnostics. Biosensors and Bioelectronics, 26 (4), 1332-1336.

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Link to published version:: https://doi.org/10.1016/j.bios.2010.07.042

Abstract

A highly sensitive method of spectroscopic ellipsometry in total internal reflection mode (TIRE) was exploited for detecting β-amyloid peptide (Aβ1–16) in the direct immune reaction with monoclonal DE2 antibodies (raised against Aβ1–16) electrostatically immobilised on the surface of gold. A rapid detection of Aβ1–16 in a wide range of concentrations from 5 μg/ml down to 0.05 ng/ml was achieved using a cost-effective and label-free direct immunoassay format. TIRE dynamic spectral measurements proved that the immune reaction between DE2 monoclonal antibodies and Aβ1–16 is highly specific with the affinity constant KD = 1.46 × 10−8 mol/l. The same DE2 antibodies were utilised for detection of amyloid precursor protein APP770, a larger protein containing Aβ1–16 domain, using the quartz crystal microbalance (QCM) measurements in liquid. A combination of QCM and TIRE kinetics results allowed the evaluation of the originally unknown concentration of APP770 in complete medium solution containing other proteins, salts, and amino acids.

Item Type: Article
Research Institute, Centre or Group - Does NOT include content added after October 2018: Biomedical Research Centre
Materials and Engineering Research Institute > Advanced Coatings and Composites Research Centre > Electronic Materials and Sensors Research Group
Identification Number: https://doi.org/10.1016/j.bios.2010.07.042
Page Range: 1332-1336
Depositing User: Ann Betterton
Date Deposited: 16 Feb 2011 09:41
Last Modified: 18 Mar 2021 10:15
URI: https://shura.shu.ac.uk/id/eprint/3140

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