A quartz crystal microbalance (QCM) serving as a biosensor to detect the target biomolecules (analytes) often suffers from the time consuming process, especially in the case of diffusion-limited reaction. In this experimental work, we modify the reaction chamber of a conventional QCM by integrating into the multi-microelectrodes to produce electrothermal vortex flow which can efficiently drive the analytes moving toward the sensor surface, where the analytes were captured by the immobilized ligands. The microelectrodes are placed on the top surface of the chamber opposite to the sensor, which is located on the bottom of the chamber.
View Article and Find Full Text PDFBiochem Biophys Res Commun
January 2012
Atomic force microscopy (AFM) is a vital instrument in nanobiotechnology. In this study, we developed a method that enables AFM to simultaneously measure specific unbinding force and map the viral glycoprotein at the single virus particle level. The average diameter of virus particles from AFM images and the specificity between the viral surface antigen and antibody probe were integrated to design a three-stage method that sets the measuring area to a single virus particle before obtaining the force measurements, where the influenza virus was used as the object of measurements.
View Article and Find Full Text PDFWe investigate a immunoassay biosensor that employs a Quartz Crystal Microbalance (QCM) to detect the specific binding reaction of the (Human IgG1)-(Anti-Human IgG1) protein pair under physiological conditions. In addition to experiments, a three dimensional time domain finite element method (FEM) was used to perform simulations for the biomolecular binding reaction in microfluidic channels. In particular, we discuss the unsteady convective diffusion in the transportation tube, which conveys the buffer solution containing the analyte molecules into the micro-channel where the QCM sensor lies.
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