A diselenium-bridged covalent organic framework with pH/GSH/photo-triple-responsiveness for highly controlled drug release toward joint chemo/photothermal/chemodynamic cancer therapy.

Here, a novel joint chemo/photothermal/chemodynamic therapy was developed using a pH/GSH/photo triple-responsive 2D-covalent organic framework (COF) drug carriers for passive target treatment of tumors with extraordinarily high efficiency. The well-designed COF (DiSe-Por) with simultaneous dynamic diselenium and imine bonds, synthesized by the copolymerization of 4,4'-diselanediyldibenzaldehyde (DiSe) with 5,10,15,20-(tetra-4-aminophenyl)-porphyrin (Por) via Schiff base chemistry, which was applied as the host for effective encapsulation and highly controlled release of anticancer drug (DOX), was stable under normal physiological settings and can effectively accumulate in tumor sites. After being internalized into the tumor cells, the unique microenvironment i.e., acidic pH and overexpressed GSH, triggered substantial degradation of DiSe-Por-DOX, promoting DOX release to kill the cancer cells. Meanwhile, the breaking of Se-Se bonds boosted the generation of intracellular ROS, disturbing the redox balance of tumor cells. The highly extended 2D structure endowed the drug delivery system with significant photothermal performance. The rise of temperature with external laser irradiation (808 nm) further promoted drug release. Additionally, the phototherapy effect was further augmented after the loading of DOX, guaranteeing an almost complete drug release to tumor tissue. As a result, the triple-responsive drug delivery system achieved a synergistic amplified therapeutic efficacy with a growth inhibitory rate of approximately 93.5% for the tumor xenografted in nude mice. Moreover, the body metabolizable and clearable DiSe-Por-DOX presented negligible toxicities toward major organs in vivo. All these characteristics verified the great potential of DiSe-Por-DOX nanosheets for multi-modality tumor treatment, accelerating the application range of COFs in biomedical fields.

A visible-light-responsive molecularly imprinted polyurethane for specific detection of dibenzothiophene in gasoline.

Dibenzothiophene and its derivatives in gasoline and diesel would release sulfur oxides during combustion, and this is harmful to human health and the environment. This paper reports a method based on a visible-light-responsive molecularly imprinted polyurethane (VMIPU) to monitor trace dibenzothiophene in gasoline. The VMIPU was prepared by a polyaddition reaction using N,N-bis-(2-hydroxyethyl)-4-phenylazoaniline as the functional monomer, dibenzothiophene as the template molecule, diphenylmethane diisocyanate as the crosslinker and castor oil as the chain extender. The VMIPU showed good visible-light-response and specific adsorption for dibenzothiophene. The trans → cis photoisomerization rate constant of azobenzene chromophores in the VMIPU shows a linear relationship with the dibenzothiophene concentration in the range of 0-20 µmol L-1. This was used to estimate trace dibenzothiophene in spiked gasoline with recoveries of 95.7-101.0% and relative standard deviations of 7.0-12.7%.

Protection of telomeres 1 (POT1) of Pinus tabuliformis bound the telomere ssDNA.

Protection of telomeres 1 (POT1) is a telomeric protein that binds to the telomere single-stranded (ss) region. It plays an essential role in maintaining genomic stability in both plants and animals. In this study, we investigated the properties of POT1 in Pinus tabuliformis Carr. (PtPOT1) through electrophoretic mobility shift assay. PtPOT1 harbored affinity for telomeric ssDNA and could bind plant- and mammalian-type ssDNA sequences. Notably, there were two oligonucleotide/oligosaccharide binding (OB) folds, and OB1 or OB2 alone, or both together, could bind ssDNA, which is significantly different from human POT1. Based on our data, we hypothesized that the two OB folds of PtPOT1 bound the same ssDNA. This model not only provides new insight into the ssDNA binding of PtPOT1 but also sheds light on the functional divergence of POT1 proteins in gymnosperms and humans.