Studies of defects in YVO<SUB>4</SUB>:Pb<SUP>2+</SUP>, Eu<SUP>3+</SUP> red phosphor material

Doubly doped YVO4:Pb2+, Eu3+ red phosphor materials with fixed Eu3+ concentration (5 mol%) and varying Pb2+ concentration were prepared via a self-propagating (combustion) synthesis. This consisted of bringing a saturated aqueous solution of the desired metal salts and a suitable organic fuel to the boil, until the mixture ignited and a self-sustaining and rather fast combustion reaction initiated, resulting in dry, amorphous or usually crystalline fine particles of the desired material. The formation of crystalline vanadates was confirmed by X-ray diffraction. A strong emission line at 619 nm due to the 5D0 &#8594; 7F2 transition in the red region was observed. Defects, created by gamma radiation, were studied by means of photoluminescence, thermally stimulated luminescence (TSL) and electron spin resonance. Photoluminescence studies display considerable reduction in emission intensity which appears to arise due to the formation of defect centres after irradiation. The defect centres formed in the present system are tentatively assigned to F+ centres and step annealing measurements suggest a connection between these centres and the TSL glow peak

Selective posttranslational inhibition of CaVβ1-associated voltage-dependent calcium channels with a functionalized nanobody

Ca2+ influx through high-voltage-activated calcium channels (HVACCs) controls diverse cellular functions. A critical feature enabling a singular signal, Ca2+ influx, to mediate disparate functions is diversity of HVACC pore-forming α1 and auxiliary CaVβ1-CaVβ4 subunits. Selective CaVα1 blockers have enabled deciphering their unique physiological roles. By contrast, the capacity to post-translationally inhibit HVACCs based on CaVβ isoform is non-existent. Conventional gene knockout/shRNA approaches do not adequately address this deficit owing to subunit reshuffling and partially overlapping functions of CaVβ isoforms. Here, we identify a nanobody (nb.E8) that selectively binds CaVβ1 SH3 domain and inhibits CaVβ1-associated HVACCs by reducing channel surface density, decreasing open probability, and speeding inactivation. Functionalizing nb.E8 with Nedd4L HECT domain yielded Chisel-1 which eliminated current through CaVβ1-reconstituted CaV1/CaV2 and native CaV1.1 channels in skeletal muscle, strongly suppressed depolarization-evoked Ca2+ influx and excitation-transcription coupling in hippocampal neurons, but was inert against CaVβ2-associated CaV1.2 in cardiomyocytes. The results introduce an original method for probing distinctive functions of ion channel auxiliary subunit isoforms, reveal additional dimensions of CaVβ1 signaling in neurons, and describe a genetically-encoded HVACC inhibitor with unique properties