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We, for the first time, systematically investigated the crystal structures, adsorption properties, and microscopic mechanism of CO 2 capture with ethylenediamine (en)-appended isostructural M 2 (dobpdc) materials (M = Mg, Sc-Zn), using spin polarized density functional theory (DFT) calculations. The binding energies of en range from 142 to 210 kJ/mol. The weakest binding materials are en-Cr 2 (dobpdc) and en-Cu 2 (dobpdc). Two typical models, the pair model and the chain model, have been considered for CO 2 adsorption. Generally, the chain model is more stable than the pair model. The CO 2 adsorption energies of the chain model are in the range of 30-96 kJ/mol, with a strong metal dependence. Among these, the en-Sc 2 (dobpdc) and en-Cu 2 (dobpdc) have the highest and lowest CO 2 adsorption energies, respectively. Moreover, the dynamic progress of CO 2 adsorption has been unveiled via exploration of the full reaction pathway, including transition states and intermediates. First, the CO 2 molecule interacts with en-MOFs to form a physisorbed complex with a shallow potential well. This is followed by overcoming a relatively large energy barrier to form a chemisorbed complex. Finally, ammonium carbamate is formed along the one-dimensional channels within the pore with a small energy barrier for configuration transformation. These results agree well with the experimental observations. Understanding the detailed microscopic mechanism of CO 2 capture is quite crucial for improving our fundamental knowledge base and potential future applications. This work will improve our understanding of CO 2 adsorption with amine functionalized MOFs. We expect our results to stimulate future experimental and theoretical research and advance the development of this field.

Detections of telomerase activity in vitro and in living cells are of great importance for clinical diagnosis of cancer. In this work, an AIEgens-based bioprobe with two fluorescent signals for enhanced monitor of extracellular and intracellular telomerase activity is designed. After addition of telomerase, two positively charged AIEgens (Silole-R and TPE-H) bind to quencher group labeled primer (QP) and the extension repeated units, leading enhancement of two telomerase-triggered fluorescent signals. Furthermore, by combination the wider linear range in vitro and lower background in living cells imaging, the bioprobe is used to detect telomerase extracted from various cell lines (MCF-7, HeLa, E-J, and HLF), 50 bladder cancer patients' urine samples, 10 normal people's urine samples, and also applied in mapping telomerase activity inside living cells (MCF-7, HeLa, MDA-MB-231, and HT1080). The results show that this well-designed strategy can successfully detect telomerase activity in vitro and in living cells with high sensitivity, indicating the potential application of this method in cancer cells bioimaging and clinical cancer diagnosis.

Herein, we report a novel strategy to accelerate the rate of DNA strand replacement reaction (DSRR) by polar organic solvents. DSRR plays a vital role in DNA nanotechnology but prolonged reaction time limits its further advancement. That is why it is extremely important to speed up the rate of DSRR. In this work, we introduce different polar organic solvents in both simple and complicated DSRR systems and observe that the rate constant is much more than in aqueous buffer. The rate acceleration of DSRR by polar organic solvents is very obvious and we believe that this strategy will extend the application of DNA nanotechnology in future.

Extracellular high-mobility group box-1 (HMGB-1) has been implicated in the inflammation response leading to the precancerous lesions of non-small cell lung cancer (NSCLC). However, the role of HMGB-1 in the inflammation response in normal human bronchial epithelial (NHBE) cells and its underlying mechanisms were still not fully understood. In this study, the inflammation response in NHBE cells was stimulated by 2.5, 5, and 10 μg/ml HMGB-1. However, the receptor for advanced glycation end products (RAGE) blocker RAGE-Ab (5 μg/ml) or 10 μM c-Jun N-terminal kinases (JNK) inhibitor SP600125 could inhibit HMGB1-induced the release of inflammation cytokines including TNF-α, IL-8, IL-10, and MCP-1 in a dose-dependent manner. Furthermore, HMGB1-induced RAGE protein expression, JNK and NF-κB activation were attenuated by the pretreatment with RAGE-Ab or JNK inhibitor SP600125 in Western blot analysis. Our data indicated that HMGB-1 induced inflammation response in NHBE cells through activating RAGE/JNK/NF-κB pathway. HMGB-1 could act as a therapeutic target for inflammation leading NHBE cells to the precancerous lesions of NSCLC.