Biomedical subjects

Satoka Aoyagi

Publications and source records attributed to Satoka Aoyagi.

4 recordsLinked to original sources

PubMed2006

Electrical oscillation at a water/octanol interface in a hydrophobic container.

The electrical potential oscillation at and the shape of the water/octanol interface were investigated using hydrophobic fluoroplastic containers. The interfacial potential between a water solution containing 1.5 mM sodium dodecyl sulfate (SDS) and an octanol solution containing 5 mM tetrabutylammonium chloride oscillated with an amplitude of 50-100 mV. The potential oscillation was also observed using a transparent fluoroplastic tube. The water/octanol interface shape was unchanged and no interfacial flow was observed during the oscillation. The interface shape was convex toward the octanol phase for 1.5 mM SDS, meaning that SDS adsorption to the wall was suppressed by the hydrophobic container. Therefore, the octanol system in a hydrophobic container enabled us to elucidate the electrical oscillation without any influence from the wall effect.

Journal Article↗

PubMed2005

Effective monitoring of protein reaction on glass plate surfaces by TOF-SIMS.

Time-of-flight secondary ion mass spectrometry (TOF-SIMS) is capable of chemically visualizing proteins on insulated samples. Distribution of an immobilized probe protein, fluorescent-labeled protein A-immobilized on a glass plate, and that of a sample protein, immunogloblin G (IgG) in solution, reacting with protein A on the biosensor surface, were evaluated with TOF-SIMS (TFS-2100, Physical Electronics). TOF-SIMS spectra and images of the protein on the glass plates were obtained, and this "mutual information", as defined by information theory, was employed to analyze the TOF-SIMS spectra of proteins. Fragment ions from protein A and IgG were distinguished by the mutual, reinforcing information and specific fragment ions to each protein were selected to obtain the TOF-SIMS image of the protein. It is evident from the TOF-SIMS images of each protein that protein A was immobilized on the substrate homogeneously and that the reaction between the immobilized protein A and IgG is not localized in this condition. Chemical images of the proteins by TOF-SIMS will contribute to a better understanding of the reaction on the biosensor surface, and thus will help the development of more sophisticated biosensors. In addition, the requisite chemical conditions as well as the interaction between the biosensor surface and the immobilized proteins were investigated by TOF-SIMS by means of sets of reinforcing, mutually supportive information.

Adsorption↗

PubMed2005

Development of fluorescence change-based, reagent-less optic immunosensor.

A reagent-less, regenerable and portable optic immunosensor was developed. A model sample, immunoglobulin G (IgG), was detected with this system based on changes in fluorescent intensity of fluorescent labeled protein A with specific reactivity to IgG depending on a reaction between the proteins. A glass plate immobilized with Qdot-labeled protein A was placed on the top of optic fibers designed for both excitation and fluorescence emission. The optic fibers with the Qdot-labeled protein A-immobilized glass plate were inserted into a solution of pH 7.4 phosphate buffered saline. After stabilization of the fluorescence intensity, IgG was added and the time-course of the fluorescence intensity was measured on a fluorometer connected with the optic fibers. Furthermore, the fluorescence response of a transient state was evaluated with the same system. When the Qdot-labeled protein A bound to IgG, fluorescence intensity decreased because of the inhibition by IgG. The degree of fluorescence decrease depends on the IgG concentration at a steady state and also in a transient state.

Antigen-Antibody Complex↗

PubMed2003

Reagentless and regenerable immunosensor for monitoring of immunoglobulin G based on non-separation immunoassay.

Based on the enhancement of fluorescein isothiocyanate (FITC) fluorescence caused by reactions between proteins, we developed a reagentless, regenerable and rapid immunosensing system to determine immunoglobulin G (IgG). Fluorescence intensity of the immobilized FITC depends on IgG concentration, ranging from 10 to 50 microg/ml, specifically, even with co-existing proteins. The response time is 30 min during steady-state measurement and is less than a minute during transient measurement. When the FITC-labeled protein A binds to IgG, the surrounding atmosphere of FITC becomes hydrophobic. Since the fluorescence intensity of fluorescent substances generally increases at a hydrophobic environment, FITC fluorescence intensity increases with the concentration of protein A bonding to IgG. This system is regenerable because the fluorescence enhancement repeatedly occurs every time the immobilized fluorescent reagent is immersed in sample solutions.

Biosensing Techniques↗