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Fabrication and characterization of a GaN/(4H)SiC vertical pn power diode using direct and interfaced epitaxial-growth approaches

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Journal of Semiconductors 2013年第4期34卷 20-23页

作者： bose srikanta Mazumder S K Laboratory for Energy and Switching-Electronics Systems Department of Electrical and Computer EngineeringUniversity of Illinois at ChicagoChicagoIL:60607USA

We report the fabrication and characterization of a vertical pn power diode which is realized using two separate epitaxial-growth mechanisms：（a） p-GaN over p-（4H）SiC, and （b） p-GaN over n-（4H）SiC with A1N as the interface layer. In all of the cases, n＋-doped （4H）SiC serves as the cathode substrate. Pd（200 A）/Au（10000 A） is used for the anode contact while Ni（1000A） is used for the bottom cathode contact. The measured forward drop of the pn diode with A1N as the interface material is found to be around 5.1 V; whereas, it is 3 V for the other sample structure. The measured reverse-blocking voltage is found to be greater than 200 V.

关键词： GaN (4H)SiC vertical pn power diode power electronics

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Analysis of curcumin interaction with human serum albumin using spectroscopic studies with molecular simulation

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Frontiers in Biology 2017年第3期12卷 199-209页

作者： Turban Kar Pijush Basak srikanta Sen Rittik Kumar Ghosh Maitree Bhattacharyya Department of Biochemistry University of Calcutta 35 Ballygunge Circular Road Kolkata-700019 West Bengal India Jagadis bose National Science Talent Search Kolkata-700107 India 229A/230 Mira Tower Lake Town Block-A Kolkata-700089 India

BACKGROUND： Curcumin has emerged to be utilized as a superb beneficial agent, due to its naturally occurring anti-oxidant, anti-inflammatory and anti-carcinogenic property. METHODS： The interaction of curcumin with human serum albumin, the main in vivo transporter of exogenous substances, was investigated using absorption spectroscopy, steady-state fluorescence, excited state life-time studies and circular dichroism ***：Isothermal titration calorimetry techniques inferred one class of binding site with binding constant -1.74 × 10^5 M ^-1 revealing a strong interaction. The binding profile was analyzed through the evaluation of the thermodynamic parameters, which indicated the involvement of hydrophobic interactions （burial of non-polar group）. Fluorescence lifetime of tryptophan residue was observed to decrease to 1.94 ns from 2.84 ns in presence of Curcumin. Percentage of ct helicity of human serum albumin was also reduced significantly upon binding with curcumin as evidenced by circular dichroism measurement leading to conformational modification of the protein molecule. CONCLUSIONS： On the basis of such complementary results, it may be concluded that curcumin shows strong binding affinity for human serum albumin, probably at the hydrophobic cavities of the protein and at or around the tryptophan residue. Molecular Docking analysis of liSA and curcumin provided light on the number of binding sites at an atomic level, which were already determined at a molecular level in spectroscopic measurements. Our study unfolds the modes of interaction of curcumin with human serum albumin in the light of different biophysical techniques and molecular modeling analysis.

关键词： curcumin human serum albumin fluorescence quenching conformational change thermodynamic parameters

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