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- 저자 : Bui Nguyen Quoc Trinh (검색결과 3 건)
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Nguyen Thi Minh Hong,Nguyen Ba Doan,Nguyen Huy Tiep,Le Viet Cuong,Bui Nguyen Quoc Trinh,Pham Duc Thang,김동현 한국물리학회 2013 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.63 No.3
In this work, we study the magnetic properties of a CoFe/NiFe/PZT heterostructured nanocompositethat is affected by the strain in the PZT substrate when a voltage in the range from –250to 250 V is applied. An interesting electric-voltage-controlled magnetic anisotropy, with a relativeincrease in magnetization up to above 100%, is observed. This brings a new challenge to operate alow-power-consuming spin electronic device. We also utilize a theoretical model based on interfacecharge-mediated and strain-mediated magnetic-electric coupling to understand the change in themagnetic properties of the investigated material.
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High-Frequency Interdigitated Array Electrode-Based Capacitive Biosensor for Protein Detection
Tuan Vu Quoc,Viet Nguyen Ngoc,Tung Thanh Bui,Chun-Ping Jen,Trinh Chu Duc 한국바이오칩학회 2019 BioChip Journal Vol.13 No.4
This paper reports a study on developing of a protein detection biochip based on interdigitated array electrodes (IDAEs) capacitive immunosensor. The protein after being preconcentrated in a detection region will be selectively captured and detected by the capacitive immunosensor. Using electrical impedance spectroscopy operated at high-frequency in the range of 100 kHz–1 MHz, the capacitance of the gold electrode is determined and the antibody surface modification steps can be also monitored. The experiment results show the capacitance changes in accordance with the adding biochemical layer on gold electrodes for each step of the antibody surface modification. In particular, the total impedance operated at 1 MHz frequency has been seen to change from 2.1 kΩ of bare chip (before antibody surface modification) to 8 kΩ after antibody surface modification process while the serial capacitance is recorded to reduce steadily from 450 pF to 55 pF. Also, the efficiency of protein chip was investigated by implementing the measurement of 10 µM BSA with and without preconcentration process. The measurement results have shown the sensitivity increasing significantly after the protein is preconcentrated in this chip. The results demonstrate high efficiency of protein detection can be achieved by operating high frequency capacitive measurement on IDAEs capacitive immunosensor.
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Tran Thi Huyen,Ha Phuong Trang,Nguyen Thi-Ngan,Bui Dinh-Thanh,Le Pham Tan Quoc,Trinh Ngoc Nam 한국수산과학회 2023 Fisheries and Aquatic Sciences Vol.26 No.3
The thermolabile haemolysin (tlh) of Vibrio parahaemolyticus (Vptlh) from V. parahaemolyticus is a multiple-function enzyme, initially describes as a haemolytic factor activated by lecithin and phospholipase A2 enzymatic activity (Shinoda, 1991; Vazquez-Morado, 2021; Yanagase et al., 1970). Until now, the tlh structure has hypothesized including N-terminal and C-terminal domain, but what domain of the Vptlh structure does the haemolytic activity has not been refined yet. In this study, a 450-bp VpTLH nucleotide sequence of the entire Vptlh gene encoded the C-terminal domain cloned firstly to examine its responsibility in the activity of the Vptlh. The C-terminal domain fused with a 6-His-tag named the His-tag-VpC-terminal domain was expressed successfully in soluble form in the BL21 (DE3) PlysS cell. Remarkably, both expression and purification results confirmed a high agreement in the molecular weight of the His-tag-VpC-terminal domain was 47 kDa. This work showed the His-tag-VpC-terminal domain lysed the erythrocyte membranes in the blood agar and the phosphate buffered saline (0.9%) media without adding the lecithin substrate of the phospholipase enzyme. Haemolysis occurred at all tested diluted concentrations of His-tag-VpC-terminal domain (p < 0.05), providing evidence for the independent haemolytic activity of the His-tag-VpC-terminal domain. The content of 100 μg of the His-tag-VpC-terminal domain brought the highest haemolytic activity of 80% compared to that in the three remaining contents. Significantly, the His-tag-VpC-terminal domain demonstrated not to involve the phospholipase activity in Luria-Bertani agar supplemented with 1% (vol/vol) egg yolk emulsion. All results proved the vital responsibility of the His-tag-VpC-terminal domain in causing the haemolytic activity without the required activation by the phospholipase enzyme. Raw extracts of Phellinus igniarus and Phellinus pipi at 10–1 mg/mL inhibited the haemolytic activity of the His-tag-VpC-terminal domain from 67.7% to 87.42%, respectively. Hence applying the His-tag-VpC-terminal domain as a simple biological material to evaluate quickly potential derivatives against the Vptlh in vivo conditions will accessible and more advantageous than using the whole of the Vptlh.
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