Interfacing Aptamer-Modified Nanopipettes with Neuronal Media and Brain Tissue.

Aptamer-functionalized biosensors exhibit high selectivity for monitoring neurotransmitters in complex environments. We translated nanoscale aptamer-modified nanopipette sensors to detect endogenous dopamine release and . These sensors employ quartz nanopipettes with nanoscale pores (ca.

Electrochemical Reduction of LaO, NdO, and CeO in LiCl-LiO Melt.

The reduction of pellets composed of individual CeO, NdO and a LaO-NdO-CeO mixture by lithium extracted on a cathode during lithium chloride electrolysis at 650 °C was studied. The methods of cyclic voltammetry, electron microscopy, including determination of the elemental composition of the studied objects, and X-ray diffraction analysis were applied for the present study. The reduction degree of rare-earth metal (REM) oxides was determined using both the bromine method and reduction melting of the samples in the graphite crucible.

[Biologically Active Peptides Isolated from Dill Anethum graveolens L].

Peptide mixtures with molecular weights of 1000-2000 Da and in vivo membrano-trophic activity against mouse hepatocyte culture at very low concentrations were isolated from dill Anethum graveolens L. leaves. It has been found that plant peptides in aqueous solution formed larger nanosized particles of approximately 90 nm with a secondary structure mainly composed of β-structures and random coil structures.

In vivo analysis of conserved C. elegans tomosyn domains.

Neurosecretion is critically dependent on the assembly of a macromolecular complex between the SNARE proteins syntaxin, SNAP-25 and synaptobrevin. Evidence indicates that the binding of tomosyn to syntaxin and SNAP-25 interferes with this assembly, thereby negatively regulating both synaptic transmission and peptide release. Tomosyn has two conserved domains: an N-terminal encompassing multiple WD40 repeats predicted to form two β-propeller structures and a C-terminal SNARE-binding motif.

Tomosyn negatively regulates CAPS-dependent peptide release at Caenorhabditis elegans synapses.

The syntaxin-interacting protein tomosyn is thought to be a key regulator of exocytosis, although its precise mechanism of action has yet to be elucidated. Here we examined the role of tomosyn in peptide secretion in Caenorhabditis elegans tomosyn (tom-1) mutants. Ultrastructural analysis of tom-1 mutants revealed a 50% reduction in presynaptic dense-core vesicles (DCVs) corresponding to enhanced neuropeptide release.