| AVS 63rd International Symposium & Exhibition | |
| Biomaterial Interfaces | Wednesday Sessions |
| Session BI+MI-WeM |
| Session: | Biosensors and Diagnostics |
| Presenter: | Kaho Kamada, Osaka University, Japan |
| Authors: | K. Kamada, Osaka University, Japan T. Ono, Osaka University, Japan Y. Kanai, Osaka University, Japan Y. Ohno, Tokushima University, Japan K. Maehashi, Tokyo University of Agriculture and Technology, Japan K. Inoue, Osaka University, Japan Y. Watanabe, Kyoto Prefectural University of Medicine, Japan T. Kawahara, Chubu University, Japan Y. Suzuki, Chubu University, Japan S. Nakakita, Kagawa University, Japan K. Matsumoto, Osaka University, Japan |
| Correspondent: | Click to Email |
A lot of the anti-influenza virus drugs such as Tamiflu® and Relenza® prevent the viruses from infecting to the next cell. Influenza viruses enter the host cells of the throat and trachea by binding to the host cell’s surface receptor molecules which contains sialic acid. After the proliferation into the cell, the viruses cleave the sialo oligosaccharides by the action of the enzyme neuraminidase (NA), and propagated viruses are detached from the cells on the infection to the next cell. Therefore, it is possible to suppress the chain of propagation of virus by inhibiting the NA. Currently, the evaluation of antiviral drugs has been conducted mainly using cultured cells, there are problems in accuracy and quantitative property. In addition, it is difficult to evaluate the mechanism of reaction. Therefore we aim to build a useful new biological model platform for drug evaluation and drug discovery research. We modified sialoglycoprotein chain on the graphene surface, and fabricated the glycan-functionalized Graphene Field-Effect Transistors (G-FET), which reproduce cell surface environment on the graphene. The reaction behavior of the virus is highly detected as the current by the G-FET. So we can quantitatively evaluate drug reaction by the physical indicators. As a first step here, we electrically measured NA reaction by the glycan-functionalized G-FET.
G-FET was produced by evaporating the electrodes on graphene obtained by the exfoliation method. 1-Pirenbutan acid succinimidyl ester as a linker, was modified human sialoglycoprotein chain having a modified amino group on the graphene channel. After dropping the NA on it, we measured time course of the neuraminidase reaction monitored by the graphene-FET.
When dropping the NA, the current value is decreased exponentially. This is because the sialic acid negatively charged was disconnected from the sugar chain, and the hole carriers induced on graphene were decreased. The rate of decrease in current value with neuraminidase dropping is in good agreement with the activity value obtained by the absorption method (A NA molecule cuts the 1.7 of molecules per second). This shows that the rate constant obtained from electrically measurement by G-FET reflects the enzyme reaction rate.
This study has received the support of JST・CREST.