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Integrating aggregation‐induced emission (AIE) into thermally activated delayed fluorescence (TADF) emitters holds great promise for the advancement of highly efficient organic light emitting diodes (OLEDs). Despite recent advancements, a thorough comprehension of the underlying mechanisms remains imperative for the practical application of such materials. In this work, we introduce a novel approach aimed at modulating the TADF process by manipulating dynamic processes in excited states through aggregation effect. Our findings reveal that aggregation not only enhances both prompt and delayed fluorescence simultaneously but also imposes constraints on molecular reorientation. This constraint reinforces spin‐orbit coupling and reduces the energy gap between singlets and triplets. These insights deepen our understanding of the fundamental mechanisms governing the aggregation effect on TADF materials and provide valuable guidance for the design of high‐efficiency photoluminescent materials. [ABSTRACT FROM AUTHOR]

Ubiquitin (Ub)‐like protein ISG15 (interferon‐stimulated gene 15) regulates innate immunity and links with the evasion of host response by viruses such as SARS‐CoV‐2. Dissecting ISGylation pathways recently received increasing attention which can inform related disease interventions, but such studies necessitate the preparation and development of various ISG15 protein tools. Here, we find that the leader protease (Lbpro) encoded by foot‐and‐mouth disease virus can promote ligation reactions between recombinant ISG15 and synthetic glycyl compounds, generating protein tools such as ISG15‐propargylamide and ISG15‐rhodamine110, which are needed for cellular proteomic studies of deISGylases, and the screening and evaluation of inhibitors against SARS‐CoV‐2 papain‐like protease (PLpro). Furthermore, this strategy can be also used to load ISG15 onto the lysine of a synthetic peptide through an isopeptide bond, and prepare Ub and NEDD8 (ubiquitin‐like protein Nedd8) protein tools. [ABSTRACT FROM AUTHOR]

Ruthenium (Ru) has been theoretically considered a viable alkaline hydrogen evolution reaction electrocatalyst due to its fast water dissociation kinetics. However, its strong affinity to the adsorbed hydroxyl (OHad) blocks the active sites, resulting in unsatisfactory performance during the practical HER process. Here, we first reported a competitive adsorption strategy for the construction of SnO2 nanoparticles doped with Ru single‐atoms supported on carbon (Ru SAs‐SnO2/C) via atomic galvanic replacement. SnO2 was introduced to regulate the strong interaction between Ru and OHad by the competitive adsorption of OHad between Ru and SnO2, which alleviated the poisoning of Ru sites. As a consequence, the Ru SAs‐SnO2/C exhibited a low overpotential at 10 mA cm−2 (10 mV) and a low Tafel slope of 25 mV dec−1. This approach provides a new avenue to modulate the adsorption strength of active sites and intermediates, which paves the way for the development of highly active electrocatalysts. [ABSTRACT FROM AUTHOR]

Photocatalytic oxidation of methanol on various anatase TiO2 nanocrystals was studied by in situ and time‐resolved characterizations and DFT calculations. Surface site and resulting surface adsorbates affect the surface band bending/bulk‐to‐surface charge migration processes and interfacial electronic structure/interfacial charge transfer processes. TiO2 nanocrystals predominantly enclosed by the {001} facets expose a high density of reactive fourfold‐coordinated Ti sites (Ti4c) at which CH3OH molecules dissociate to form the CH3O adsorbate (CH3O(a)Ti4c). CH3O(a)Ti4c localized density of states are almost at the valence band maximum of TiO2 surface, facilitating the interfacial hole transfer process; CH3O(a)Ti4c with a high coverage promotes upward surface band bending, facilitating bulk‐to‐surface hole migration. CH3O(a)Ti4c exhibits the highest photocatalytic oxidation rate constant. TiO2 nanocrystals enclosed by the {001} facets are most active in photocatalytic methanol oxidation. [ABSTRACT FROM AUTHOR]

Ubiquitin (Ub)‐like protein ISG15 (interferon‐stimulated gene 15) regulates innate immunity and links with the evasion of host response by viruses such as SARS‐CoV‐2. Dissecting ISGylation pathways recently received increasing attention which can inform related disease interventions, but such studies necessitate the preparation and development of various ISG15 protein tools. Here, we find that the leader protease (Lbpro) encoded by foot‐and‐mouth disease virus can promote ligation reactions between recombinant ISG15 and synthetic glycyl compounds, generating protein tools such as ISG15‐propargylamide and ISG15‐rhodamine110, which are needed for cellular proteomic studies of deISGylases, and the screening and evaluation of inhibitors against SARS‐CoV‐2 papain‐like protease (PLpro). Furthermore, this strategy can be also used to load ISG15 onto the lysine of a synthetic peptide through an isopeptide bond, and prepare Ub and NEDD8 (ubiquitin‐like protein Nedd8) protein tools. [ABSTRACT FROM AUTHOR]