Uniform anatase TiO2 nanocuboids enclosed by active {100} and {001} facets over a wide size range (60–830 nm in length) with controllable aspect ratios were solvothermally synthesized through hydrolysis of titanium tetraisopropoxide (TTIP) using acetic acid (HAc) as the solvent and the ionic liquid 1‐butyl‐3‐methylimidazolium tetrafluoroborate ([bmim][BF4]) as the capping agent. The size and aspect ratio of the anatase TiO2 nanocuboids can be readily adjusted by changing the composition parameters including the contents of [bmim][BF4], water, and HAc in the quaternary solution system. It was revealed that [bmim][BF4] played an important role in stabilizing both the {100} and {001} facets of the anatase TiO2 nanocuboids. On the one hand, [bmim][BF4] acted as a fluoride source to release F− ions for stabilizing the {001} facets; on the other hand, the [bmim]+ ions acted as effective capping ions to preferentially stabilize the {100} facets. The obtained near‐monodisperse anatase TiO2 nanocuboids exhibited an interesting self‐assembly behavior during deposition. These single‐crystalline anatase nanocuboids showed extremely high crystalline phase stability, retaining the pure phase of anatase as well as the morphology even after being calcined at 900 °C. Moreover, the anatase nanocuboids exhibited considerably enhanced photocatalytic activity owing the wholly exposed active {100} and {001} facets.

Toll-like receptor (TLR) signaling is pivotal to innate and adaptive immune responses and must be tightly controlled. The mechanisms of TLR signaling have been the focus of extensive studies. Here we report that the tripartite-motif protein TRIM30alpha, a RING protein, was induced by TLR agonists and interacted with the TAB2-TAB3-TAK1 adaptor-kinase complex involved in the activation of transcription factor NF-kappaB. TRIM30alpha promoted the degradation of TAB2 and TAB3 and inhibited NF-kappaB activation induced by TLR signaling. In vivo studies showed that transfected or transgenic mice overexpressing TRIM30alpha were more resistant to endotoxic shock. Consistent with that, in vivo 'knockdown' of TRIM30alpha mRNA by small interfering RNA impaired lipopolysaccharide-induced tolerance. Finally, expression of TRIM30alpha depended on NF-kappaB activation. Our results collectively indicate that TRIM30alpha negatively regulates TLR-mediated NF-kappaB activation by targeting degradation of TAB2 and TAB3 by a 'feedback' mechanism.