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1.
Nanotechnology ; 30(32): 325201, 2019 Aug 09.
Artículo en Inglés | MEDLINE | ID: mdl-30991363

RESUMEN

Lateral memristors configured with inert Pt contacts and mixed phase tin oxide layers have exhibited immediate, forming-free, low-power bidirectional resistance switching. Activity dependent conductance and relaxation in the low resistance state resembled short term potentiation in biological synapses. After scanning probe microscopy, x-ray photoelectron spectroscopy and electrical measurements, the device characteristics were attributed to Joule heating induced decomposition of the minority SnO phase and formation of a SnO2 conducting filament with higher effective n-type doping. Finally, the devices recognized input voltage pulse sequences and spectral data by returning unique conductance states, suggesting suitability for bio-inspired pattern recognition systems.

2.
Nanoscale ; 16(28): 13551-13561, 2024 Jul 18.
Artículo en Inglés | MEDLINE | ID: mdl-38949653

RESUMEN

Possessing excellent electronic properties and high chemical stability, semiconducting n-type two-dimensional (2D) tin dioxide (SnO2) nanosheets have been featured in sensing and electrocatalysis applications recently. Derived from non-layered crystal structures, 2D SnO2 has abundant unsaturated dangling bonds existing at the surface, providing interfacial activity. How the surface chemistry alters the electronic properties of 2D SnO2 nanomaterials remains unexplored. In this study, we synthesised ultra-thin 2D SnO2 nanosheets using a liquid metal (LM) touch printing technique and investigated experimentally and theoretically how the interactions of organic solvents composed of alkyl and hydroxyl groups with the surface of LM-derived 2D SnO2 modulate the electronic properties. It was found that alkane solvents can physically absorb onto the SnO2 surface with no impact on the material conductivity. Alcohol-based solvents on the other hand interact with the SnO2 surface via chemical absorptions primarily, in which oxygen atoms of hydroxyl groups in the alcohols form bonds with the surface atoms of SnO2. The binding stability is determined by the length and configuration of the hydrocarbon chain in alcohols. As representative long-chain alcohols, 1-octanol and 1-pentanol attach onto the SnO2 surface strongly, lowering the binding energy of Sn4+ and reducing the electron transfer ability of SnO2 nanosheets. Consequently, the electronic properties, i.e. conductivity and electronic mobility of SnO2 nanosheet-based electronic devices are decreased significantly.

3.
Anal Chim Acta ; 1279: 341787, 2023 Oct 23.
Artículo en Inglés | MEDLINE | ID: mdl-37827635

RESUMEN

Polydimethyl glutarimide (PMGI) layers with sub-micron thicknesses have been modified in a 2.5 kV Ar plasma immersion ion implantation (PIII) process to introduce free radical covalent binding sites. The surface roughness of the PMGI increased after the PIII treatment but no through-layer defects were observed. When applied to the treated PMGI, horseradish peroxidase (HRP) enzyme remained bound to the surface after extended immersion in sodium dodecyl sulfate solution (SDS). Hence, covalent binding between the activated surface and enzyme was confirmed. This covalent binding was achieved up to 24-h after the PIII process. The treated PMGI was then incorporated as a gate dielectric layer within a lateral three-terminal electrolyte-gated device. The device output characteristics resembled those of post-synaptic outputs; as successive (pre-synaptic) voltage pulses were applied to the gate, paired pulse depression and spike rate dependent plasticity were observed in the source-drain (post-synaptic) current. These characteristics were altered by the presence of HRP immobilised on the plasma-modified PMGI gate dielectric layer thus providing readout detection. These results and preliminary device characteristics show the potential for the plasma functionalized PMGI as a sensitive and reproducible biosensing technology.


Asunto(s)
Piperidonas , Dodecil Sulfato de Sodio , Enzimas Inmovilizadas/química , Iones , Peroxidasa de Rábano Silvestre/química
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