Frequency change of piezoelectric quartz crystals in contact with solutions and development of latex piezoelectric immunoassay (LPEIA)

Kurosawa, Shigeru; Muratsugu, Makoto; Kitajima, Hideo; Ogawa, Yoshihiko; Nemoto, Eiji; Kamo, Naoki

doi:10.1016/0925-4005(93)85163-5

Cited by 1 publication

(1 citation statement)

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“…Subsequently, Thompson and co-workers , interpreted the frequency responses of TSM devices immersed in water to interfacial immunochemical reactions in terms of the viscous properties of the protein layer, rather than changes in mass or bulk solution properties. More recent times have seen the further use of TSM devices, in various forms, for the detection of interfacial immunochemical reactions − and of nucleic acid hybridization. , In many of these studies large discrepancies between experimental values and predictions of mass uptake generated through the Sauerbrey expression were found, although these observations did not appear to deter the various authors from invoking the mass-response dogma. Interestingly, in another study of the kinetics of protein adsorption a closer correlation between frequency changes and alteration of the double-layer capacitance of the underlying electrode was found …”

Section: Introductionmentioning

confidence: 99%

Interfacial Properties of Biotin Conjugate−Avidin Complexes Studied by Acoustic Wave Sensor

Ghafouri

Thompson

1998

Langmuir

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The adsorption of avidin, neutravidin, and biotin-labeled dextran 10,000, dextran 70,000, bovine albumin, and insulin to the gold electrodes of thickness-shear-mode acoustic wave devices was studied in a flow injection analysis configuration. Electrodes with different surface rugosity and free energy were also examined. Changes in series resonance frequency for the various molecules as a result of electrode adsorption cannot be explained in terms of the conventional mass-response effect. Perturbation of the properties of the protein and polysaccharide layers, such as their viscosity, and acoustic coupling phenomena offer a more reasonable basis to evaluate the results. In an analogous fashion, the acoustic wave sensor signals obtained for the formation of the various avidin-and neutravidin-biotin conjugate samples do not correspond to the additional mass deposited on the device surface. The responses for the binding of biotinylated insulin to avidin and to the nonglycosylated form of the parent molecule were completely different. This result is ascribed to a difference of surface free energy associated with the two protein-based interfaces. The acoustic wave sensor was also employed to investigate the formation of avidin-biotin conjugate multilayer structures on the surface of the device. Multilayer buildup is detectable for several pairs of avidin-biotin interactions, but the corresponding shifts in series resonance frequency gradually diminish in magnitude. Finally, the introduction of biotin itself appears to result in structural changes in the multilayer deposit, causing alterations in viscoelastic properties.

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