No abstract

Nuclear translocation of human H‐chain in its intact cage‐like structure without any additional modifications enables a rapid nuclear delivery of an encapsulated anticancer drug (doxorubicin). This reduces the doses of drugs simultaneously bypassing the cellular multidrug resistance. Apoferritin exhibits synergistic effects through attenuating drug‐induced dysregulation of the cellular iron. Tests on cerebellar organotypic cultures show the natural cell selectivity and drug accumulation in brain tissue.

The first specific functionality of the light-chain (L-chain) subunit of the universal iron storage protein ferritin was identified. The electrons released during iron-oxidation were transported across the ferritin cage specifically through the L-chains and the inverted electron transport through the L-chains also accelerated the demineralization of ferritin.

A selective and specific inhibition of the catalase mimetic activity but not SOD-like activity of Pt-apoferritin can be achieved through the choice of the inhibitor. The recovery of activity using a reducing agent was explored and proven to successfully restore the surface-chemistry of NPs.

nanomaterials with biological enzymelike catalytic activity. Since the pioneering work by Yan and co-workers [1] that showed chemically inert Fe 3 O 4 nanoparticles possess unexpected peroxidase-like activity, countless nanomaterial-based artificial enzymes (named nanozyme) were developed to imitate the catalytic functions of oxidases, [2] peroxidases, [3] superoxide dismutase, [4] and catalase. [5] Owing to their merits of simple synthesis procedure with low cost, good stability, multiple functions, as well as good robustness under extreme conditions, nanozymes have been considered as next-generation synthetic enzymes and attracted great attention worldwide. [6] Unlike natural enzymes, the enzymemimicking activities of nanozymes can be modulated by the size, morphology, composition, as well as surface engineering with numerous strategies. [7] In consequence, stimulatory or inhibitory effects on enzyme mimetic activities can be realized due to changes in surface physical and electronic properties, active sites accessibility, substrates affinity, and production desorption. Nevertheless, the currently reported methods still lack activity specificity, which always simultaneously accelerate or decrease multiple activities. This, to some extent, hampers its further application closely related to specific and desired nanozymatic activity.Recently, gold nanozyme has gained special interest due to its unique physiochemical and optical characteristics and exhibits high utilization value in biomedical applications. As both peroxidase and catalase mimetics, its relatively low activities were upregulated by a serial of modulators, such as bovine serum albumin, ATP, hemin, ions, metals, and carbon nanomaterials. [3b,8] In particular, some heavy metal ions like Ag + , Bi 3+ , and Hg 2+ were demonstrated to be the promising activators to reveal remarkable enhancement in enzyme-like activities. [9] For instance, the catalase-like activity of AuNPs was strongly increased by over hundred-fold after surface deposition of Hg 2+ . [10] However, the possible interactions between metal ions and gold, as well as the exact activation mechanism remain unclear and need to be fully elucidated. More seriously, the heavy metal ions accelerate simultaneously both peroxidase and catalase activity, which is harmful if only one specific activity is desired. Taking nanozymatic-catalytic therapy

Light-chain apoferritin lacks ferroxidase activity, which can be supplemented with Pt-nanoparticles. The hybrid bioinorganic nanoparticle outperforms its heavy-chain pendant in terms of ferroxidase activity, mineralization ability and inhibition resistance. Being active in a cellular environment it regulates the iron homeostasis.

No abstract

A serie of tetrahydroquinolines were synthesized in good yields using the Povarov reaction and evaluated as inhibitors of Acetilcholinesterase in vitro. The most active compounds showed an IC 50 of 193µg/mL, the analysis of result suggest modification in the patters of substitution to increassed activity.