The
ability to confine and manipulate light below the diffraction
limit is a major goal of future multifunctional optoelectronic/plasmonic
systems. Here, we demonstrate the design and realization of a tunable
and localized electrical source of excitons coupled to surface plasmons
based on a polymer light-emitting field-effect transistor (LEFET).
Gold nanorods that are integrated into the channel support localized
surface plasmons and serve as nanoantennas for enhanced electroluminescence.
By precise spatial control of the near-infrared emission zone in the
LEFET via the applied voltages the near-field coupling between electrically
generated excitons and the nanorods can be turned on or off as visualized
by a change of electroluminescence intensity. Numerical calculations
and spectroscopic measurements corroborate significant local electroluminescence
enhancement due to the high local density of photonic states in the
vicinity of the gold nanorods. Importantly, the integration of plasmonic
nanostructures hardly influences the electrical performance of the
LEFETs, thus, highlighting their mutual compatibility in novel active
plasmonic devices.
Sarco-endoplasmic reticulum Ca2+-ATPase (SERCA), a P-type ATPase that sustains Ca2+ transport and plays a major role in intracellular Ca2+ homeostasis, represents a therapeutic target for cancer therapy. Here, we investigated whether ruthenium-based anticancer drugs, namely KP1019 (indazolium [trans-tetrachlorobis(1H-indazole)ruthenate(III)]), NAMI-A (imidazolium [trans-tetrachloro(1H-imidazole)(S-dimethylsulfoxide)ruthenate(III)]) and RAPTA-C ([Ru(η6-p-cymene)dichloro(1,3,5-triaza-7-phosphaadamantane)]), and cisplatin (cis-diammineplatinum(II) dichloride) might act as inhibitors of SERCA. Charge displacement by SERCA adsorbed on a solid-supported membrane was measured after ATP or Ca2+ concentration jumps. Our results show that KP1019, in contrast to the other metal compounds, is able to interfere with ATP-dependent translocation of Ca2+ ions. An IC50 value of 1 μM was determined for inhibition of calcium translocation by KP1019. Conversely, it appears that KP1019 does not significantly affect Ca2+ binding to the ATPase from the cytoplasmic side. Inhibition of SERCA at pharmacologically relevant concentrations may represent a crucial aspect in the overall pharmacological and toxicological profile of KP1019.
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