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In this paper, hierarchical CuO nanoflowers were prepared by a facile, controllable and low-cost method. The structure and morphology of the CuO nanoflowers were characterized by scanning electron microscopy, X-ray diffraction spectroscopy, nitrogen adsorption–desorption isotherm and X-ray photoelectron spectroscopy measurements. CuO nanoflowers were then immobilized on the surface of a glassy carbon electrode to develop a nonenzymatic sensor for simultaneous detection of hydrogen peroxide and glucose. Electrochemical measurements demonstrated that the sensor showed good response toward H2O2 with a high sensitivity of 956.69 μA mM−1 cm−2 and a wide linear range of 0.005–14.07 mM. Moreover, the nonenzymatic sensor also exhibited excellent electrocatalytic activity toward glucose oxidation with a high sensitivity of 1086.34 μA mM−1 cm−2 and a low detection limit of 0.12 μM (S/N = 3). This study paves a new way for the construction of nonenzymatic sensors.

An ultrasensitive and high-performance electrochemical nitrite sensing platform based on gold nanoparticles deposited on poly (dimethyl diallyl ammonium chloride)-decorated MXene (Ti3C2Tx) (AuNPs/Ti3C2Tx-PDDA) was constructed. AuNPs/Ti3C2Tx-PDDA on the surface of electrode displayed synergetic catalytic effect for oxidizing NO2‾ originating from especially catalytic activity of AuNPs, large area and excellent conductivity of Ti3C2Tx, as well as electrostatic interaction of PDDA. The amperometry technique was employed for quantitative determination of nitrite, in which the AuNPs/Ti3C2Tx-PDDA/GCE sensing platform showed outstanding linear relationship in 0.1–2490 μM and 2490–13490 μM for nitrite, meanwhile the detection limit of 0.059 μM. Besides, the prepared sensor possessed high sensitivity of 250 μA mM−1 cm−2 yet excellent selectivity, stability and reproducibility. Furthermore, this platform also exhibited satisfactory feasibility of nitrite sensing in running water and ham sausage sample. This work would broaden a facile approach to construct high sensitivity electrochemical sensing platform via two-dimension materials and its nanocomposites.

Pituitary adenylate cyclase-activating polypeptide (PACAP) is a potential therapeutic peptide with anti-inflammatory and anti-oxidative effects. In order to increase the efficiency of traversing biological barriers, a novel fusion peptide PACAP-TAT was produced by tagging PACAP at its C-terminus with 11-amino acid TAT protein transduction domain. The results of characteristic assays showed that PACAP-TAT activated PACAP specific receptor PAC1 with the same potency as PACAP and PACAP-TAT crossed blood-brain barrier (BBB), blood-air barrier (BAB) and blood-testis barrier (BTB) with the efficiency about 2.5-fold higher than that of PACAP. Both PACAP-TAT and PACAP were used treat the mice with lung injury induced by repeated smoke inhalation. It was shown that both PACAP-TAT and PACAP decreased the mortality, increased the body weight and inhibited the edema and vascular permeability in the lungs of the mice received repeated smoke inhalation, while PACAP-TAT displayed more marked effects than PACAP. PACAP-TAT decreased myeloperoxidase (MPO) activity, increased catalase (CAT) activity and down-regulated interleukin 6 (IL-6) and malondialdehyde (MDA) levels in the lungs with a significantly higher efficiency than PACAP. The histopathological analysis also showed that PACAP-TAT attenuated the cell filtration and bronchi epithelial hyperplasia more significantly than PACAP. Moreover the leukocyte count in blood and the serum superoxide dismutase (SOD) activity in the mice treated with PACAP-TAT were significantly different from that in mice treated with PACAP (p0.05). All these data indicated that PACAP-TAT with increased traversing ability was more effective than PACAP in protecting the mice from the lung injury induced by repeated smoke inhalation.

Pituitary adenylate cyclase-activating polypeptide (PACAP) is a potential therapeutic neuropeptide. The 11-amino acid human immunodeficiency virus TAT protein transduction domain is able to deliver protein cargoes across the cell membrane and the blood-brain barrier. A novel fusion protein PACAP-TAT, containing TAT at the C-terminus of PACAP was therefore produced and studied for the ability to cross blood barriers. The gene encoding PACAP-TAT was cloned into the expression vector pKYB, and the target peptide PACAP-TAT was purified using the Intein Mediated Purification with an Affinity Chitin-binding Tag (IMPACT) system. The results of cell assays showed that PACAP-TAT stimulated the cell viability of PAC1-CHO cells with the same potency as PACAP, which indicated that the fusion of TAT did not affect the ability of PACAP-TAT to activate the PACAP-specific receptor PAC1. The transfer efficiencies of PACAP-TAT and PACAP across the blood-brain barrier (BBB), blood-air barrier (BAB) and blood-testis barrier (BTB) were assayed using peptides labeled with fluorescein isothiocyanate (FITC). The results showed that PACAP-TAT traversed blood barriers with an efficiency approximately 2.5-fold greater than PACAP. Fluorescence microscopic examination showed that PACAP-TAT traversed the BBB significantly more efficiently than PACAP. Furthermore, intraperitoneal (i.p.) injection of PACAP-TAT induced a stronger inhibitory effect on food intake than PACAP (p