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Magnetic acoustic resonance immunoassay (MARIA): a multifrequency acoustic approach for the non‐labelled detection of biomolecular interactions
Author(s) -
ArayaKleinsteuber Bernardita,
Roque Ana C. A.,
Kioupritzi Eleftheria,
Stevenson Adrian C.,
Lowe Christopher R.
Publication year - 2006
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.790
Subject(s) - immunoassay , covalent bond , surface acoustic wave , substrate (aquarium) , resonator , biosensor , quartz , nanotechnology , detector , materials science , chemistry , mars exploration program , quartz crystal microbalance , adsorption , optoelectronics , acoustics , optics , antibody , physics , composite material , oceanography , organic chemistry , immunology , biology , geology , astronomy
A unique sensing platform, comprising an electromagnetic field detector and an acoustic resonator, has been used as a wireless system for remote sensing of biorecognition events. The MARS (Magnetic Acoustic Resonator Sensor) technique has proven useful for detecting the formation of protein multilayers derived from specific binding phenomena. The technique enables multifrequency analysis, without the need of electrodes attached to the sensing element, and also facilitates the in situ surface modification of the substrate for antibody attachment. The MARS sensor was utilized as the platform on which a standard immunoassay was carried out. Two different conditions for the attachment of the first antibody to the quartz surface were tested: (i) Adsorption of the antibody onto the surface of a bare quartz disc; (ii) covalent immobilization of the antibody to a chemically modified quartz surface. Both methods can be successfully utilized for the ‘label‐less’ detection of the biorecognition event between goat IgG and anti‐goat IgG by analysis of the multifrequency spectrum. Covalent attachment of the primary antibody results in a more efficient immobilization, with higher surface density, and a consistently enhanced response for the binding of the secondary antibody. This approach will be of interest to life scientists and biochemists that require high performance assay methodologies that do not use chemical labels. Copyright © 2006 John Wiley & Sons, Ltd.