Enhanced Stabilities and Production Yields of MAPbBr3 Quantum Dots and Their Applications as Stretchable and Self-Healable Color Filters.

Organic-inorganic hybrid CH3NH3PbBr3 (MAPbBr3) perovskite quantum dots (PQDs) are considered as promising and cost-effective building blocks for various optoelectronic devices. However, during centrifugation for the purification of these PQDs, commonly used polar protic and aprotic non-solvents (e.g., methanol and acetone) can destroy the nanocrystal structure of MAPbBr3 perovskites, which will significantly reduce the production yields and degrade the optical properties of the PQDs. This study demonstrates the use of methyl acetate (MeOAc) as an effective non-solvent for purifying as-synthesized MAPbBr3 PQDs without causing severe damage, which facilitates attainment of stable PQD solutions with high production yields. The MeOAc-washed MAPbBr3 PQDs maintain their high photoluminescence (PL) quantum yields and crystalline structures for long periods in solution states. MeOAc undergoes a hydrolysis reaction in the presence of the PQDs, and the resulting acetate anions partially replace the original surface ligands without damaging the PQD cores. Time-resolved PL analysis reveals that the MeOAc-washed PQDs show suppressed non-radiative recombination and a longer PL lifetime than acetone-washed and methanol-washed PQDs. Finally, it is demonstrated that a composite of the MAPbBr3 PQDs and a thermoplastic elastomer (polystyrene-block-polyisoprene-block-polystyrene) is feasible as a stretchable and self-healable green color filter for a white light-emitting diode device.

Conformational Dynamics and Functional Implications of Phosphorylated ß-Arrestins.

Arrestins desensitize and/or internalize G-protein-coupled receptors by interacting with phosphorylated receptors. A few studies have reported that arrestins themselves can be phosphorylated, and the phosphorylation status modulates their cellular functions. However, the effects of phosphorylation on arrestin structure have not been studied. Here, we investigated the conformational changes in ß-arrestin-1 and -2 upon incorporation of phospho-mimetic mutations into the known phosphorylation sites (i.e., S412D for ß-arrestin-1 and S14D, T276D, S14D/T276D, S361D, T383D, and S361D/T383D for ß-arrestin-2) by using hydrogen/deuterium-exchange mass spectrometry (HDX-MS). HDX-MS analysis suggested that ß-arrestin-2 S14D/T276D shows an HDX profile similar to the pre-active states, resulting in increased interaction with receptors. Phospho-mimetic mutation at corresponding residues of ß-arrestin-1 (i.e., S13D/T275D) induced similar conformational and functional consequences, and the detailed structural changes related to ß-arrestin-1 S13D/T275D were investigated further by X-ray crystallography.

Efficient Debundling of Few-Walled Carbon Nanotubes by Wrapping with Donor-Acceptor Polymers for Improving Thermoelectric Properties.

Organic thermoelectric (TE) materials have great potential as sustainable energy sources for powering flexible and wearable electronic devices via harvesting of human body heat. Recent advances in soluble conjugated polymer/carbon nanotube (CNT) composites have facilitated achievement of high TE power factors. However, the effects of conjugated polymers on the debundling and electrical percolation of CNTs and on the TE properties of their composites are not yet fully understood. Herein, we introduce a novel type of polymer/CNT composite composed of a donor-acceptor (D-A)-type polymer and few-walled CNTs (FWCNTs). Three kinds of D-A polymers are employed to disperse FWCNTs, and the photophysical, morphological, and TE properties of the resulting polymer/FWCNT composites are compared with those of composites composed of FWCNTs dispersed with conventional donor-only poly(3-hexylthiophene). The results reveal that the strong intermolecular interaction forces and high backbone planarity of the D-A polymers facilitate effective debundling of FWCNTs, which results in much smaller bundle sizes. Consequently, the D-A polymer/FWCNT composite films show superior electrical percolation and TE performances with improved power factors of up to 459 µW/mK2. Finally, we demonstrate the feasibility of the D-A polymer/FWCNT composites for use in the fabrication of a flexible TE generator, which shows a maximum power output of 210 nW at a temperature gradient of 20 K.

Role of Helix 8 in Dopamine Receptor Signaling.

G protein-coupled receptors (GPCRs) are membrane receptors whose agonist-induced dynamic conformational changes trigger heterotrimeric G protein activation, followed by GRK-mediated phosphorylation and arrestin-mediated desensitization. Cytosolic regions of GPCRs have been studied extensively because they are direct contact sites with G proteins, GRKs, and arrestins. Among various cytosolic regions, the role of helix 8 is least understood, although a few studies have suggested that it is involved in G protein activation, receptor localization, and/or internalization. In the present study, we investigated the role of helix 8 in dopamine receptor signaling focusing on dopamine D1 receptor (D1R) and dopamine D2 receptor (D2R). D1R couples exclusively to Gs, whereas D2R couples exclusively to Gi. Bioinformatic analysis implied that the sequences of helix 8 may affect GPCR-G protein coupling selectivity; therefore, we evaluated if swapping helix 8 between D1R and D2R changed G protein selectivity. Our results suggest that helix 8 is not involved in D1R-Gs or D2R-Gi coupling selectivity. Instead, we observed that D1R with D2R helix 8 or D1R with an increased number of hydrophobic residues in helix 8 relative to wild-type showed diminished ß-arrestin-mediated desensitization, resulting in increased Gs signaling.

Structural basis of recognition and destabilization of the histone H2B ubiquitinated nucleosome by the DOT1L histone H3 Lys79 methyltransferase.

DOT1L is a histone H3 Lys79 methyltransferase whose activity is stimulated by histone H2B Lys120 ubiquitination, suggesting cross-talk between histone H3 methylation and H2B ubiquitination. Here, we present cryo-EM structures of DOT1L complexes with unmodified or H2B ubiquitinated nucleosomes, showing that DOT1L recognizes H2B ubiquitin and the H2A/H2B acidic patch through a C-terminal hydrophobic helix and an arginine anchor in DOT1L, respectively. Furthermore, the structures combined with single-molecule FRET experiments show that H2B ubiquitination enhances a noncatalytic function of the DOT1L-destabilizing nucleosome. These results establish the molecular basis of the cross-talk between H2B ubiquitination and H3 Lys79 methylation as well as nucleosome destabilization by DOT1L.