Bioinspired hydrogels have promising prospects in applications such as wearable devices, human health monitoring equipment, and soft robots due to their multifunctional sensing properties resembling natural skin. However, the preparation of intelligent hydrogels that provide feedback on multiple electronic signals simultaneously, such as human skin receptors, when stimulated by external contact pressure remains a substantial challenge. In this study, we designed a bioinspired hydrogel with multiple conductive capabilities by incorporating carbon nanotubes into a chelate of calcium ions with polyacrylic acid and sodium alginate. The bioinspired hydrogel consolidates self-healing ability, stretchability, 3D printability, and multiple conductivities. It can be fabricated as an integrated strain sensor with simultaneous piezoresistive and piezocapacitive performances, exhibiting sensitive (gauge factor of 6.29 in resistance mode and 1.25 kPa–1 in capacitance mode) responses to subtle pressure changes in the human body, such as finger flexion, knee flexion, and respiration. Furthermore, the bioinspired strain sensor sensitively and discriminatively recognizes the signatures written on it. Hence, we expect our ideas to provide inspiration for studies exploring the use of advanced hydrogels in multifunctional skin-like smart wearable devices.
Glucose stimulates insulin secretion from pancreatic  cells by inducing the recruitment and fusion of insulin vesicles to the plasma membrane. However, little is currently known about the mechanism of the initial docking or tethering of insulin vesicles prior to fusion. Here, we examined the role of the SEC6-SEC8 (exocyst) complex, implicated in trafficking of secretory vesicles to fusion sites in the plasma membrane in yeast and in regulating glucose-stimulated insulin secretion from pancreatic MIN6  cells. We show first that SEC6 is concentrated on insulin-positive vesicles, whereas SEC5 and SEC8 are largely confined to the cytoplasm and the plasma membrane, respectively. Overexpression of truncated, dominant-negative SEC8 or SEC10 mutants decreased the number of vesicles at the plasma membrane, whereas expression of truncated SEC6 or SEC8 inhibited overall insulin secretion. When single exocytotic events were imaged by total internal reflection fluorescence microscopy, the fluorescence of the insulin surrogate, neuropeptide Y-monomeric red fluorescent protein brightened, diffused, and then vanished with kinetics that were unaffected by overexpression of truncated SEC8 or SEC10. Together, these data suggest that the exocyst complex serves to selectively regulate the docking of insulin-containing vesicles at sites of release close to the plasma membrane.
A facile approach of layer-by-layer depositing and hydrolysis of FeCl3 is developed to fabricate 3D-ordered Fe2O3 film. The 3D-ordered Fe2O3 film was characterized by SEM, XRD, and DRUV−vis. It has 3D-ordered interconnecting macropores (340 nm) with nanocrystalline hematite Fe2O3 walls (27.2 nm). The 3D-ordered macroporous nanocrystalline Fe2O3 film exhibits 2.4 times larger photocatalytic activity for the photodegradation of dye in the presence of H2O2 under visible irradiation than the nanocrystalline α-Fe2O3 film without macropores and very good photostability. The much higher photocatalytic activity of the 3D-ordered macroporous nanocrystalline Fe2O3 film than that of the reference Fe2O3 film is attributed to the unique nanostructure and architecture of the 3D-ordered Fe2O3 film, which result in the much greater light harvesting efficiency and efficient mass transport in the former than in the latter due to the existence of 3D-ordered interconnecting macropores. The effect of photonic stop band on the photocatalytic activity of the 3D-ordered Fe2O3 film was studied by angle-dependent solid-state photodegradation experiments with monochromatic irradiation. A slow photon enhancement of photocatalytic activity was achieved by adjusting the red edge of the photonic stop band of the 3D-ordered Fe2O3 film close to the electronic bandgap of Fe2O3. The photodegradation mechanism of crystal violet on the 3D-ordered Fe2O3 photocatalyst in the presence or absence of H2O2 was discussed.
Eu-doped pollucite CsAlSi2O6 was synthesized by the sol-gel method and heated in an air atmosphere. The crystal structure and the microstructure of the phosphors were investigated by X-ray powder diffraction and SEM images, respectively. The photoluminescence spectra and temperature dependent decay curves were measured. An abnormal reduction phenomenon of Eu(3+) → Eu(2+) was reported when Eu(3+) ions were doped in alkaline metal cation sites in CsAlSi2O6 prepared in an oxidizing atmosphere. The abnormal mechanism was discussed on the basis of the charge compensation model and a rigid three-dimensional framework structure of CsAlSi2O6. The luminescence color centers were investigated by luminescence decay lifetimes and thermal stabilities of Eu(2+) ions. The defect complexes of [(Eu(3+)Cs)(••)-2VCs'] or [(Eu(3+)Cs)(••)-Oi″] induced by the substitution of Eu(3+) on Cs(+) were suggested in the lattices. Eu(2+) ions could be regarded as Eu(3+) ions combining with the released electrons from defects Oi″ or VCs' in close vicinity of Eu(3+) (Eu(3+) + e); the electrons cannot enter the atom track of Eu(2+) presenting luminescence of Eu(2+) ions. The results indicate that several defect traps can be attributed to the abnormal reduction mechanism of Eu(3+) to Eu(2+) ions in a matrix.
Tumor tissues/cells are the best sources of antigens to prepare cancer vaccines. However, due to the difficulty of solubilization and delivery of water‐insoluble antigens in tumor tissues/cells, including water‐insoluble antigens into cancer vaccines and delivering such vaccines efficiently to antigen‐presenting cells (APCs) remain challenging. To solve these problems, herein, water‐insoluble components of tumor tissues/cells are solubilized by 8 m urea and thus whole components of micrometer‐sized tumor cells are reasssembled into nanosized nanovaccines. To induce maximized immunization efficacy, various antigens are loaded both inside and on the surface of nanovaccines. By encapsulating both water‐insoluble and water‐soluble components of tumor tissues/cells into nanovaccines, the nanovaccines are efficiently phagocytosed by APCs and showed better therapeutic efficacy than the nanovaccine loaded with only water‐soluble components in melanoma and breast cancer. Anti‐PD‐1 antibody and metformin can improve the efficacy of nanovaccines. In addition, the nanovaccines can prevent lung cancer (100%) and melanoma (70%) efficiently in mice. T cell analysis and tumor microenvironment analysis indicate that tumor‐specific T cells are induced by nanovaccines and both adaptive and innate immune responses against cancer cells are activated by nanovaccines. Overall, this study demonstrates a universal method to make tumor‐cell‐based nanovaccines for cancer immunotherapy and prevention.
We have identified YkbA from Bacillus subtilis as a novel member of the L-amino acid transporter (LAT) family of amino acid transporters. The protein is ϳ30% identical in amino acid sequence to the light subunits of human heteromeric amino acid transporters. Purified His-tagged YkbA from Escherichia coli membranes reconstituted in proteoliposomes exhibited sodium-independent, obligatory exchange activity for L-serine and L-threonine and also for aromatic amino acids, albeit with less activity. Thus, we propose that YkbA be renamed SteT (Ser/Thr exchanger transporter). Kinetic analysis supports a sequential mechanism of exchange for SteT. Freeze-fracture analysis of purified, functionally active SteT in proteoliposomes, together with blue native polyacrylamide gel electrophoresis and transmission electron microscopy of detergent-solubilized purified SteT, suggest that the transporter exists in a monomeric form.Freeze-fracture analysis showed spherical particles with a diameter of 7.4 nm. Transmission electron microscopy revealed elliptical particles (diameters 6 ؋ 7 nm) with a distinct central depression. To our knowledge, this is the first functional characterization of a prokaryotic member of the LAT family and the first structural data on an APC (amino acids, polyamines, and choline for organocations) transporter. SteT represents an excellent model to study the molecular architecture of the light subunits of heteromeric amino acid transporters and other APC transporters.The APC (amino acids, polyamines, and choline for organocations) superfamily of transport proteins includes nearly 250 members that function as solute-cation symporters and solutesolute antiporters (1). They occur in all phyla from prokaryotes to higher eukaryotes and vary in length between 350 and 850 amino acid residues. The smaller proteins are generally of prokaryotic origin, whereas the larger ones are of eukaryotic origin and have N-and C-terminal hydrophilic extensions. Most APC members are predicted to possess 12 transmembrane (TM)The L-amino acid transporter (LAT) family belongs to the APC superfamily. LAT family members correspond to the light subunits of the heteromeric amino acid transporters (HATs), also called glycoprotein-associated amino acid transporters (2-4). HATs are composed of two subunits, a polytopic membrane protein (the light subunit) and a disulfide-linked N-glycosylated type II membrane glycoprotein (the heavy subunit). The light subunit is the catalytic component of the transporter, whereas the heavy subunit appears to be essential only for trafficking to the plasma membrane. Two types of heavy subunit (4F2hc and rBAT) and 10 types of light subunit have so far been *
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