Embedding an enzyme within aMOF as exoskeleton (enzyme@MOF) offers new opportunities to improve the inherent fragile nature of the enzyme,but also to impart novel biofunctionality to the MOF.D espite the remarkable stability achieved for MOF-embedded enzymes,e mbedding patterns and conversion of the enzymatic biofunctionality after entrapment by aM OF have only received limited attention. Herein, we reveal howe mbedding patterns affect the bioactivity of an enzyme encapsulated in ZIF-8. The enzyme@MOF can maintain high activity when the encapsulation process is driven by rapid enzyme-triggered nucleation of ZIF-8. When the encapsulation is driven by slow coprecipitation and the enzymes are not involved in the nucleation of ZIF-8, enzy-me@MOF tends to be inactive owing to unfolding and competing coordination caused by the ligand, 2-methyl imidazole.T hese two embedding patterns can easily be controlled by chemical modification of the amino acids of the enzymes,modulating their biofunctionality.Supportinginformation and the ORCID identification number(s) for the author(s) of this article can be found under: https://doi.

Supportinginformation and the ORCID identification number(s) for the author(s) of this article can be found under: https://doi.

Cell‐free enzymatic catalysis (CFEC) is an emerging biotechnology that enable the biological transformations in complex natural networks to be imitated. This biomimetic approach allows industrial products such as biofuels and biochemical to be manufactured in a green manner. Nevertheless, the main challenge in CFEC is the poor stability, which restricts the effectiveness and lifetime of enzymes in sophisticated applications. Immobilization of the enzymes within solid carriers is considered an efficient strategy for addressing these obstacles. Specifically, putting an “armor‐like” porous metal–organic framework (MOF) exoskeleton tightly around the enzymes not only shields the enzymes against external stimulus, but also allows the selective transport of guests through the accessible porous network. Herein we present the concept of this biotechnology of MOF‐entrapped enzymes and its cutting‐edge applications.

The International Agency for Research on Cancer (IARC) has classified outdoor air pollution and the particulate matter (PM) in outdoor air pollution as carcinogenic to humans, as based on sufficient evidence of carcinogenicity in humans and experimental animals and strong support by mechanistic studies. The data with important contributions to the evaluation are reviewed, highlighting the data with particular relevance to China, and implications of the evaluation with respect to China are discussed. The air pollution levels in Chinese cities are among the highest observed in the world today and frequently exceed health-based national and international guidelines. Data from high-quality epidemiologic studies in Asia, Europe, and North America consistently show positive associations between lung cancer and PM exposure and other indicators of air pollution, which persist after adjustment for important lung cancer risk factors, such as tobacco smoking. Epidemiologic data from China are limited but nevertheless indicate an increased risk of lung cancer associated with several air pollutants. Excess cancer risk is also observed in experimental animals exposed to polluted outdoor air or extracted PM. The exposure of several species to outdoor air pollution is associated with markers of genetic damage that have been linked to increased cancer risk in humans. Numerous studies from China, especially genetic biomarker studies in exposed populations, support that the polluted air in China is genotoxic and carcinogenic to humans. The evaluation by IARC indicates both the need for further research into the cancer risks associated with exposure to air pollution in China and the urgent need to act to reduce exposure to the population.

No abstract

This work reports a new protein-directed, hydrogen-bonded assembly strategy to organize proteins and organic linkers into robust hybrid frameworks. The pconjugated carboxylate linkers are feasible to be anchored on the peptide backbone of proteins through hydrogen-bonded interaction and then by

Polybrominated diphenyl ethers (PBDEs) have become widely distributed as environmental contaminants due to their use as flame retardants. Their structural similarity to other halogenated aromatic pollutants has led to speculation that they might share toxicological properties such as hepatic enzyme induction. In this work we synthesized a number of PBDE congeners, studied their affinity for rat hepatic Ah receptor through competitive binding assays, and determined their ability to induce hepatic cytochrome P-450 enzymes by means of EROD (ethoxyresorufin-O-deethylase) assays in human, rat, chick, and rainbow trout cells. Both pure PBDE congeners and commercial PBDE mixtures had Ah receptor binding affinities 10(-2)-10(-5) times that of 2,3,7,8-tetrachlorodibenzo-p-dioxin. In contrast with polychlorinated biphenyls, Ah receptor binding affinities of PBDEs could not be related to the planarity of the molecule, possibly because the large size of the bromine atoms expands the Ah receptor's binding site. EROD activities of the PBDE congeners followed a similar rank order in all cells. Some congeners, notably PBDE 85, did not follow the usual trend in which strength of Ah receptor binding affinity paralleled P-450 induction potency. Use of the gel retardation assay with a synthetic oligonucleotide indicated that in these cases the liganded Ah receptor failed to bind to the DNA recognition sequence.

Herein, we report the first example of using mesoporous hydrogen‐bonded organic frameworks (MHOFs) as the protecting scaffold to organize a biocatalytic cascade. The confined microenvironment of MHOFs has robust and large transport channels, allowing the efficient transport of a wide range of biocatalytic substrates. This new MHOF‐confined cascade system shows superior activity, extended scope of catalytic substrates, and ultrahigh stability that enables the operation of complex chemical transformations in a porous carrier. In addition, the advantages of MHOF‐confined cascades system for point‐of‐care biosensing are also demonstrated. This study highlights the advantages of HOFs as scaffold for multiple enzyme assemblies, which has huge potential for mimicking complex cellular transformation networks in a controllable manner.