pH-Triggered visual detection of Escherichia coli based on the co-assembly of bacitracin and thymolphthalein.

A novel probe for bacteria was simply synthesized through the solvent-induced co-assembly of bacitracin (AMP) and thymolphthalein (TP) without complicated modification. Combining with aptamer-Fe3O4, AMP/TP nanoparticles were used for the colorimetric detection of Escherichia coli with good sensitivity through the NaOH-triggered blue color and a smartphone-based App.

Bacitracin-Functionalized Dextran-MoSe2 with Peroxidase-like and Near-Infrared Photothermal Activities for Low-Temperature and Synergetic Antibacterial Applications.

Bacitracin (an antimicrobial peptide, AMP)-modified dextran-MoSe2 nanosheets (AMP/dex-MoSe2 NSs) were constructed and applied for low-temperature and synergetic antibacterial applications. The near-infrared (NIR) photothermal and peroxidase-like activities of dex-MoSe2 were combined with the bacterial membrane-binding ability of AMP through electrostatic adsorption, and a multimode antibacterial method was realized. H2O2 was converted into a hydroxyl radical (·OH) by AMP/dex-MoSe2, which exhibits a higher antibacterial activity and can avoid the toxicity of a high concentration of H2O2. Importantly, the production of ·OH and the antibacterial efficiency of AMP/dex-MoSe2 were accelerated by low-temperature heat sterilization with NIR irradiation. Owing to the AMP-guided binding and destruction effect to the bacterial membrane, AMP/dex-MoSe2 shows a better antibacterial effect on Gram-negative Escherichia coli under NIR irradiation as compared to catalytic treatment or NIR photothermal sterilization alone. Furthermore, the cytotoxicity and hemolysis of AMP/dex-MoSe2 were weak and in a relatively safe range. This multimode antibacterial strategy based on the AMP/dex-MoSe2 nanozyme will pave a way for the development of more safe and efficient antibacterial applications.

A self-correcting fluorescent assay of tyrosinase based on Fe-MIL-88B-NH2 nanozyme.

A self-correcting fluorescent assay of tyrosinase (TYR) was developed by utilization of Fe-MIL-88B-NH2 as a peroxidase-like nanozyme and a capture probe. Fe-MIL-88B-NH2 nanozyme was selected as an electron donor, and the oxidization product (dopamine-o-quinone) acts as an energy acceptor. First, TYR catalyzes the oxidation of tyramine hydrochloride to dopamine and then to dopamine-o-quinone. Second, Fe-MIL-88B-NH2 with intrinsic peroxidase-like activity decomposes H2O2 to produce ·OH radicals, which further accelerate the oxidation of dopamine to dopamine-o-quinone. Excessive H2O2 and ·OH radicals reduce the interferences from ascorbic acid at the same time providing a self-correcting ability. Dopamine-o-quinone reacts with -NH2 groups on the ligand of Fe-MIL-88B-NH2 through Michael reaction which results in fluorescence quenching. Under 365-nm excitation, the fluorescence emission intensity at 452 nm gradually decreased with increasing TYR concentration varying from 0 to 10 U mL-1. The linear range is from 1 to 5 U mL-1 and the detection limit is 0.05679 U mL-1. This self-correcting fluorescent assay of tyrosinase exhibits good sensitivity and selectivity which is also successfully applied for tyrosinase inhibitor detection. Schematic representation of fluorescent assay for tyrosinase determination based on Fe-MIL-88B-NH2 nanozyme. A self-correcting fluorescent assay for tyrosinase was developed based on the Fe-MIL-88B-NH2 nanozyme.

Accelerating the peroxidase-like activity of MoSe2 nanosheets at physiological pH by dextran modification.

Surface modification of MoSe2via dextran during ultrasound exfoliation is demonstrated to be an efficient and easy strategy to accelerate the peroxidase-like catalytic activity of MoSe2 nanosheets at neutral pH. The enhancement of catalytic activity is owing to the rich negative charges of dextran on the dextran-modified MoSe2 nanosheets.

A competitive immunoassay for electrochemical impedimetric determination of chlorpyrifos using a nanogold-modified glassy carbon electrode based on enzymatic biocatalytic precipitation.

A direct competitive impedimetric immunoassay for chlorpyrifos (CPF) was developed that is based on the specific affinity of immunoassay and the enzymatic biocatalytic precipitation amplification strategy. The CPF antibody (anti-CPF) was anchored onto an electro-deposited nanogold modified glassy carbon electrode surface by adsorption of the Au-NH2 bond and Au-SH bond. This improved the electrode reactivity and the loading amount of anti-CPF. Abundant horseradish peroxidase (HRP) and bovine serum albumin-CPF (BSA-CPF) were anchored onto spherical gold nanoparticles (AuNPs, 16 ± 2 nm) to form HRP-AuNP-BSA-CPF (analyte competitor). CPF determination was achieved when the competitive immunoassay occurred between CPF and analyte competitor with anti-CPF. In the presence of H2O2 and 4-chloro-1-naphthol, an enzyme-mediated biocatalytic precipitation process was triggered and produced an insoluble 4-chloro-1(4H)-naphthalenone. This insoluble substance increased the Faradaic impedance of the base electrode. The impedimetric signal was determined at the formal potential of 220 mV and alternating voltage of 10 mV. This signal decreased with increasing concentration of CPF over a linear range of 1.0 × 10-3 ng mL-1~10 ng mL-1 with a detection limit of 0.070 pg mL-1. The immunoassay has been tested for determination of chlorpyrifos in complex matrices such as artificially spiked vegetables with recoveries in the range 85 to 110%. The relative standard deviations were less than 7.5%. Graphical abstractSchematic representation of electrochemical impedimetric immunoassay for chlorpyrifos determination before enzymatic biocatalytic precipitation (BCP, red line) process and after BCP process (blue line).