Efficient Emission of Ultraviolet Light by Solid State Organic Fluorophores: Synthesis and Characterization of 1,4-Dialkeny-2,5-dioxybenzenes.

The design and development of organic luminophores that exhibit efficient ultraviolet (UV) fluorescence in the solid state remains underexplored. Here, we report that 1,4-dialkenyl-2,5-dialkoxybenzenes and 1,4-dialkenyl-2,5-disiloxybenzenes act as such UV-emissive fluorophores. The dialkenyldioxybenzenes were readily prepared in three steps from 2,5-dimethoxy-1,4-diacetylbenzene or 2,5-dimethoxy-1,4-diformylbenzene via two to four steps from 1,4-bis(diethoxyphosphonylmethyl)-2,5-dimethoxybenzene. The dialkenyldioxybenzenes emit UV light in solution (λem =350-387 nm) and in the solid state (λem =328-388 nm). In addition, the quantum yields in the solid state were generally higher than those in solution. In particular, the adamantylidene-substituted benzenes fluoresced in the UV region with high quantum yields (Φ=0.37-0.55) in the solid state. Thin films of poly(methyl methacrylate) doped with the adamantylidene-substituted benzenes also exhibited UV emission with good efficiency (Φ=0.27-0.45). Density functional theory calculations revealed that the optical excitation of the dialkenyldimethoxybenzenes involves intramolecular charge-transfer from the ether oxygen atoms to the twisted alkenyl-benzene-alkenyl moiety, whereas the dialkenylbis(triphenylsiloxy)benzenes were optically excited through intramolecular charge-transfer from the oxygen atoms and twisted π-system to the phenyl-Si moieties of each triphenylsilyl group.

Identification and functional characterization of novel nonsynonymous variants in the human multidrug and toxin extrusion 2-K.

This study was performed to identify genetic polymorphisms in multidrug and toxin extrusion 2-K (MATE2-K, SLC47A2), a proton/organic cation antiporter that plays a role in the transport of organic cations across the apical membrane in kidney epithelial cells into the urine, and to demonstrate their effects on MATE2-K functions in vitro. Four of the thirty single nucleotide polymorphisms (SNPs) we identified in three ethnic groups (Caucasian, African American, and Japanese) were novel [308C>G (P103R), c.487-8C>T, 818A>G (Y273C), and c.1018+14T>C]. The transport activities of the prototypical substrates, tetraethylammonium and metformin, for four nonsynonymous SNPs (P103R, P162L, G211V, and Y273C) were significantly different from those of the wild-type. In particular, transport activity was higher in P103R than in the wild-type, which is the first time elevated transport activity was demonstrated due to these coding SNPs. Kinetic analysis revealed that P103R had a higher Vmax value, whereas Y273C had a lower value than that in the wild-type. Cell surface protein expression levels were higher for P103R than for the wild-type, whereas Y273C expression was decreased. Immunofluorescence analysis revealed that the P103R protein was localized to the plasma membrane, whereas Y273C showed cytoplasmic localization. Therefore, the difference in transport activities between P103R and Y273C variants was suggested to be responsible for the different protein expression levels observed at the plasma membrane. Four nonsynonymous SNPs in this study showed relatively low allelic frequencies (0.5 to 2.1%), but these were associated with markedly reduced or increased MATE2-K function.