Abstract. In this paper, the gold nanorods (GNRs) were synthesized via a seed-mediated method by using 1-3 nm seeds-in diameter and gold atoms created from the reduced Au 3+ ions by ascorbic acid (AA) in the presence of cetyltrimethyl ammonnium bromide (CTAB) as a soft template. The aspect ratio of GNRs as well as growth yield were controlled by adjusting the concentration of Ag + ions. This method gave the formation of mono-dispersed GNRs with the controlled size and peak plasmon resonance. The UV-VIS-NIR absorption spectra and transmission electronic microscopy (TEM) images of the GNR solution showed that the plasmon absorption spectra depend on the aspect ratio of GNRs. The GNRs were also attached with bioconjugate molecules in order to be more stable and used in biomedical applications. This work also presents the results of photothermal effects of GNRs in real tissues by changing the power density of laser beam.
Understanding carrier dynamics and electromagnetic interactions between emerging quantum-confined nanostructures and plasmonic structures is crucial for future biological applications. In this research, we fabricate gold monolayer-protected clusters (AuMPC). We demonstrate enhanced light absorption and fluorescence of AuMPCs by varying the initial alkali concentration. We measure absorption bands enhanced up to nine times with extended and distinct features centered at 3.33 eV, and fluorescence enhanced up to 3.9 times. An increased alkali concentration changes the charge transfer capability of the surface thiolate ligands through sulfur-gold bonds, which in turn enhance/reduce the fluorescence intensity.
GPR88 is an orphan G-protein–coupled receptor (GPCR) highly expressed in striatal medium spiny neurons (MSN), also found in cortical neurons at low level. In MSN, GPR88 has a canonical GPCR plasma membrane/cytoplasmic expression, whereas in cortical neurons, we previously reported an atypical intranuclear localization. Molecular size analysis suggests that GPR88, expressed in plasma membrane of MSN or in nuclear compartment of cortical neurons, corresponds to the full-length protein. By transfection of cortical neurons, we showed that GPR88 fluorescent chimeras exhibit a nuclear localization. This localization is contingent on the third intracytoplasmic loop and C-terminus domains, even though these domains do not contain any known nuclear localization signals (NLS). Using yeast two-hybrid screening with these domains, we identified the nuclear proteins ATRX, TOP2B, and BAZ2B, all involved in chromatin remodeling, as potential protein partners of GPR88. We also validated the interaction of GPR88 with these nuclear proteins by proximity ligation assay on cortical neurons in culture and coimmunoprecipitation experiments on cortical extracts from GPR88 wild-type (WT) and knockout (KO) mice. The identification of GPR88 subcellular partners may provide novel functional insights for nonclassical modes of GPCR action that could be relevant in the maturating process of neocortical neurons.
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