Understanding of multi-level resistive switching mechanism in GeOx through redox reaction in H2O2/sarcosine prostate cancer biomarker detection.

Formation-free multi-level resistive switching characteristics by using 10 nm-thick polycrystalline GeOx film in a simple W/GeOx/W structure and understanding of switching mechanism through redox reaction in H2O2/sarcosine sensing (or changing Ge°/Ge4+ oxidation states under external bias) have been reported for the first time. Oxidation states of Ge0/Ge4+ are confirmed by both XPS and H2O2 sensing of GeOx membrane in electrolyte-insulator-semiconductor structure. Highly repeatable 1000 dc cycles and stable program/erase (P/E) endurance of >106 cycles at a small pulse width of 100 ns are achieved at a low operation current of 0.1 µA. The thickness of GeOx layer is found to be increased to 12.5 nm with the reduction of polycrystalline grain size of <7 nm after P/E of 106 cycles, which is observed by high-resolution TEM. The switching mechanism is explored through redox reaction in GeOx membrane by sensing 1 nM H2O2, which is owing to the change of oxidation states from Ge0 to Ge4+ because of the enhanced O2- ions migration in memory device under external bias. In addition, sarcosine as a prostate cancer biomarker with low concentration of 50 pM to 10 µM is also detected.

Negative voltage modulated multi-level resistive switching by using a Cr/BaTiOx/TiN structure and quantum conductance through evidence of H2O2 sensing mechanism.

Negative voltage modulated multi-level resistive switching with quantum conductance during staircase-type RESET and its transport characteristics in Cr/BaTiOx/TiN structure have been investigated for the first time. The as-deposited amorphous BaTiOx film has been confirmed by high-resolution transmission electron microscopy. X-ray photo-electron spectroscopy shows different oxidation states of Ba in the switching material, which is responsible for tunable more than 10 resistance states by varying negative stop voltage owing to slow decay value of RESET slope (217.39 mV/decade). Quantum conductance phenomenon has been observed in staircase RESET cycle of the memory devices. By inspecting the oxidation states of Ba+ and Ba2+ through measuring H2O2 with a low concentration of 1 nM in electrolyte/BaTiOx/SiO2/p-Si structure, the switching mechanism of each HRS level as well as the multi-level phenomenon has been explained by gradual dissolution of oxygen vacancy filament. Along with negative stop voltage modulated multi-level, current compliance dependent multi-level has also been demonstrated and resistance ratio up to 2000 has been achieved even for a thin (<5 nm) switching material. By considering oxidation-reduction of the conducting filaments, the current-voltage switching curve has been simulated as well. Hence, multi-level resistive switching of Cr/BaTiOx/TiN structure implies the promising applications in high dense, multistate non-volatile memories in near future.

A solution study on the local and global structure changes of cytochrome c: an unfolding process induced by urea.

The local and global structural changes of cytochrome c induced by urea in aqueous solution have been studied using X-ray absorption spectroscopy (XAS) and small-angle X-ray scattering (SAXS). According to the XAS result, both the native (folded) protein and the unfolded protein exhibit the same preedge features taken at Fe K-edge, indicating that the Fe(III) in the heme group of the protein maintains a six-coordinated local structure in both the folded and unfolded states. Furthermore, the discernible differences in the X-ray absorption near-edge structure (XANES) of these two states are attributed to a possible spin transition of the Fe(III) from a low-spin state to a high-spin state during the unfolding process. The perseverance of six-coordination and the spin transition of the iron are reconciled by a proposed ligand exchange, with urea and water molecules replacing the methionine-80 and histidine-18 axial ligands, respectively. The SAXS result reveals a significant morphology change of cytochrome c from a globular shape of a radius of gyration R(g) = 12.8 A of the native protein to an elongated ellipsoid shape of R(g) = 29.7 A for the unfolded protein in the presence of concentrated urea. The extended X-ray absorption fine structure (EXAFS) data unveil the coordination geometries of Fe(III) in both the folded and unfolded state of cytochrome c. An initial spin transition of Fe(III) followed by an axial ligand exchange, accompanied by the change in the global envelope, is proposed for what happened in the protein unfolding process of cytochrome c.