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A series of low-cost Lewis acidic deep eutectic solvents (DESs) was synthesized and applied for the first time for catalyzing the polymerization of α-pinene to produce terpene resins. The DES catalyst of [AlCl3]3[CPL] prepared via the self-assembly of AlCl3 and caprolactam (CPL) exhibited the highest catalytic activity, and polymerization conditions were optimized by a single-factor method: 15 g α-pinene, 3 g catalyst, 1 g initiator, −5 °C reaction temperature, and 4 h reaction time. Under these conditions, the softening point of the terpene resin reached (annular spheroid method) 118.3 °C, the acid value was 0.22 mg KOH g−1, and the depth of color (Fe–Co method) was 5. The structure of [AlCl3]3[CPL] was characterized using FT-IR, 1H-NMR, and UV-vis spectroscopy. GPC measure showed that the number-average molecular weight of the terpene resin was 510, the weight-average molecular weight was 776, and the polydispersity index was 1.523. TG results indicated that the terpene resin had favorable thermal stability. After the reaction, the product and the catalyst could be automatically divided into two phases, which was beneficial for recycling the catalyst. The results revealed that [AlCl3]3[CPL] exhibited good recyclability. [ABSTRACT FROM AUTHOR]

Aims: The basolateral amygdala (BLA) plays an integral role in anxiety disorders (such as post traumatic stress disorder) stem from dysregulated fear memory. The excitability of glutamatergic neurons in the BLA correlates with fear memory, and the afterhyperpolarization current (IAHP) mediated by small‐conductance calcium‐activated potassium channel subtype 2 (SK2) dominates the excitability of glutamatergicneurons. This study aimed to explore the effect of MPP2 interacts with SK2 in the excitability of glutamatergic neurons in the BLA and the extinction of conditioned fear in mice. Methods: Fear memory was analyzed via freezing percentage. Western blotting and fluorescence quantitative PCR were used to determine the expression of protein and mRNA respectively. Electrophysiology was employed to measure the excitability of glutamatergic neurons and IAHP. Results: Fear conditioning decreased the levels of synaptic SK2 channels in the BLA, which were restored following fear extinction. Notably, reduced expression of synaptic SK2 channels in the BLA during fear conditioning was caused by the increased activity of protein kinase A (PKA), while increased levels of synaptic SK2 channels in the BLA during fear extinction were mediated by interactions with membrane‐palmitoylated protein 2 (MPP2). Conclusions: Our results revealed that MPP2 interacts with the SK2 channels and rescues the excitability of glutamatergic neurons by increasing the expression of synaptic SK2 channels in the BLA to promote the normalization of anxiety disorders and provide a new direction for the treatment. [ABSTRACT FROM AUTHOR]

Many nanoproteases contain tetravalent metal ions and catalyze peptide‐bond hydrolysis only at high temperature (60 °C). Here, we report a new and effective strategy to explore nanoproteases from nanoparticles containing low valent metal ions. We found that flower‐like CuCoO2 nanoparticles (CuCoO2 NPs) containing low valent Cu+ possessed excellent catalytic activity towards selective cleavage of peptide bonds with hydrophobic residues in bovine serum albumin (BSA) at room temperature. CuCoO2 NPs exhibited excellent stability and had great reusability. CuCoO2 NPs also hydrolyzed heat‐denatured and surfactant‐denatured BSA. Mechanism analysis revealed that the high Lewis acidity of Co3+ and the low valence of Cu+ were both essential for the high protease activity of CuCoO2 NPs. The flower‐like structure of CuCoO2 NPs and the strong nucleophilicity of Cu+‐bound hydroxyl endow them with excellent catalytic performance. The findings open a new way for the design and discovery of high‐efficiency nanoproteases. [ABSTRACT FROM AUTHOR]

Many nanoproteases contain tetravalent metal ions and catalyze peptide-bond hydrolysis only at high temperature (60 °C). Here, we report a new and effective strategy to explore nanoproteases from nanoparticles containing low valent metal ions. We found that flower-like CuCoO 2 nanoparticles (CuCoO 2 NPs) containing low valent Cu + possessed excellent catalytic activity towards selective cleavage of peptide bonds with hydrophobic residues in bovine serum albumin (BSA) at room temperature. CuCoO 2 NPs exhibited excellent stability and had great reusability. CuCoO 2 NPs also hydrolyzed heat-denatured and surfactant-denatured BSA. Mechanism analysis revealed that the high Lewis acidity of Co 3+ and the low valence of Cu + were both essential for the high protease activity of CuCoO 2 NPs. The flower-like structure of CuCoO 2 NPs and the strong nucleophilicity of Cu + -bound hydroxyl endow them with excellent catalytic performance. The findings open a new way for the design and discovery of high-efficiency nanoproteases., (© 2023 Wiley-VCH GmbH.)

Atherosclerosis (AS) is the primary etiology of cardiovascular disease, which is considered the leading cause of death all over the world. MicroRNA miR-499-5p was involved in the functional regulation of myocardial and skeletal muscle, whereas its role in atherosclerosis, especially in vascular smooth muscle cells (VSMCs), remains unclear. Our study aims to investigate the effects of miR-499-5p in the proliferation and migration of VSMCs and potential mechanisms. We used mouse aortic vascular smooth muscle cells (MOVAS) and ApoE -/- mice to establish the models of AS in vitro and in vivo, respectively. RT-PCR was performed to detect the expression level of miR-499-5p. Subsequently, Cell Counting Kit-8 (CCK-8) assays, Transwell assays, and wound-healing assays were used to evaluate cell proliferation and migration. Dual-luciferase reporter assay was performed to validate the interaction between miR-499-5p and SOX6. miR-499-5p significantly increased in aorta tissues of mice in AS tissues and vascular smooth muscle cells treated with ox-LDL. miR-499-5p overexpression could promote the proliferation and migration of MOVAS. Bioinformatics analysis predicted and further experiments verified that miR-499-5p could directly bind to the 3'-untranslated region (UTR) region of SOX6. Further, miR-499-5p induced an increased expression of smooth muscle proliferation and migration-related genes, PCNA, cyclin D1 , and matrix metalloproteinase ( MMP2 ), as well as the decreased expression of proliferation inhibiting factor p21 , which was significantly reversed by SOX6 overexpression. miR-499-5p boosts the proliferation and migration of smooth muscle cells by binding and inhibiting SOX6 expression. The miR-499-5p/SOX6 axis may present a promising therapeutic implication for the prevention and treatment of cardiovascular diseases.