Search

Tungsten carbide (W

The rational design and exploration of the oxygen evolution reaction (OER) electrocatalysts with high efficiency, low cost, and long-term durability are extremely important for overall water splitting. Recently, numerous studies have shown that the OER reaction kinetics can be modified by optimizing components, introducing carbon matrix, and regulating porous nanostructures. Herein, a flexible and controllable electrospinning strategy is proposed to construct porous nitrogen (N)-doped carbon (C) nanofibers (NFs) with nickel-iron (NiFe) alloy nanoparticles encapsulated inside (NiFe@NCNFs) as an OER electrocatalyst. Benefiting from the strong synergistic effects that stem from the one-dimensional mesoporous structures with optimized binary metal components encapsulated in the N-doped carbon nanofibers, the NiFe@NCNFs exhibits enhanced OER performance with a low overpotential (294 mV at 10 mA cm

As an invaluable tool for biomedical research, the green fluorescent proteins (GFPs) make tumor cells, amyloid plaques, and pathogenic bacteria equally visible. Here, inspired by the chromophore of GFPs, we constructed a tyrosine-based peptide that show green luminescence in the aggregation state. Similar to the optical property of GFPs, the tyrosine-based peptidyl nanoparticles are stabilized by intermolecular hydrogen bonding and emit fluorescence when the Tyr residues bear phenolic anions. In addition, the tyrosine-based peptide is cell-permeable and endosome-escaped when conjuncted with the GPGR motif of human immunodeficiency virus and can be used for stable cell imaging due to its excellent photostability, pH-sensitivity and biocompatibility in physiological conditions. The results provide a promising pathway to construct peptidyl bioluminescent agents for biomedical applications.

Preventing the unwanted adsorption of proteins and cells at articular cartilage surfaces plays a critical role in maintaining healthy joints and avoiding degenerative diseases such as osteoarthritis. Immobilized at the surface of healthy articular cartilage is a thin, interfacial layer of macromolecules consisting mainly of hyaluronic acid (HA) and lubricin (LUB; a.k.a. PRG4) that is believed to form a co-adsorbed, composite film now known to exhibit synergistic tribological properties. Bioinspired by the composition of cartilage surfaces, composite layers of HA and LUB were grafted to Au surfaces and the antiadhesive properties were assessed using surface plasmon resonance and quartz crystal microbalance. A clear synergistic enhancement in antiadhesive properties was observed in the composite films relative to grafted HA and LUB layers alone. Atomic force microscopy (AFM) normal force measurements provide insight into the architecture of the HA/LUB composite layer and implicate a strong contribution of hydrophobic interactions in the binding of LUB end-domains directly to HA chains. These AFM force measurements indicate that the adhesion of LUB to HA is strong and indicate that the hydrophobic coupling of LUB to HA shields the hydrophobic domains in these molecules from interactions with other proteins or molecules.

A facile approach was reported to establish mimic multienzyme systems with hierarchically porous (HP) biomimetic metal–organic frameworks (MOFs) and natural enzymes for tandem catalysis. The hierarchically porous MOF HP-PCN-224(Fe) with peroxidase-like activity and tunable hierarchical porosity was synthesized via a modulator-induced strategy. HP-PCN-224(Fe) not only acts as the enzyme-immobilization matrix but also as an effective enzyme mimic, which could cooperate with the immobilized natural enzyme to catalyze the cascade reactions. The mimic multienzyme systems were used for the efficient colorimetric detection of a series of biomolecules, including glucose and uric acid. This work displays the great potential to construct highly functional biocatalysts by integrating the merits of both natural enzymes and MOF mimics, which are promising for applications in biosensing and biomimetic catalysis.

Metal-organic frameworks (MOFs), which are a unique class of hybrid porous materials built from metal ions and organic ligands, have attracted significant interest in recent years as a promising platform for controlled drug delivery. Current approaches for creating MOFs-based responsive drug carriers involve encapsulation of stimuli-responsive compositions into MOFs or postsynthetic surface modification with sensitive molecules. In this study, we developed a novel intrinsic redox-responsive MOFs carrier, MOF-M(DTBA) (M = Fe, Al or Zr) by using iron, aluminum, or zirconium as metal nodes and 4,4'-dithiobisbenzoic acid (4,4'-DTBA) as the organic ligand. The disulfide bond in 4,4'-DTBA is cleavable by glutathione (GSH), which is often overexpressed in tumor cells. It was found that MOF-Zr(DTBA) synthesized at 40 °C displayed the appropriate size and properties as a drug carrier. By incorporating curcumin (CCM) into MOF-Zr(DTBA), CCM@MOF-Zr(DTBA) nanoparticles were obtained that displayed a faster releasing behavior in vitro and enhanced the cell death compared with free CCM. The in vivo anticancer experiments indicate that CCM@ MOF-Zr(DTBA) exhibits much higher antitumor efficacy than free CCM. This strategy for constructing responsive MOFs-based nanocarriers might open new possibilities for the application of MOFs in drug delivery, molecular imaging, or theranostics.

The aim of this study was to explore the influence of amphiphilic and zwitterionic structures on the resistance of protein adsorption to peptide self-assembled monolayers (SAMs) and gain insight into the associated antifouling mechanism. Two kinds of cysteine-terminated heptapeptides were studied. One peptide had alternating hydrophobic and hydrophilic residues with an amphiphilic sequence of CYSYSYS. The other peptide (CRERERE) was zwitterionic. Both peptides were covalently attached onto gold substrates via gold-thiol bond formation. Surface plasmon resonance analysis results showed that both peptide SAMs had ultralow or low protein adsorption amounts of 1.97-11.78 ng/cm2 in the presence of single proteins. The zwitterionic peptide showed relatively higher antifouling ability with single proteins and natural complex protein media. We performed molecular dynamics simulations to understand their respective antifouling behaviors. The results indicated that strong surface hydration of peptide SAMs contributes to fouling resistance by impeding interactions with proteins. Compared to the CYSYSYS peptide, more water molecules were predicted to form hydrogen-bonding interactions with the zwitterionic CRERERE peptide, which is in agreement with the antifouling test results. These findings reveal a clear relation between peptide structures and resistance to protein adsorption, facilitating the development of novel peptide-containing antifouling materials.

Colloidosomes are promising carriers for immobilizing enzyme for catalytic purposes in aqueous/organic media. However, they often suffer from one or more problems regarding catalytic performance, stability, and recyclability. Here, we report a novel approach for the synthesis of cross-linkable colloidosomes by the selective polymerization of dopamine at oil/water interfaces in a Pickering emulsion. An efficient enzyme immobilization method was further developed by covalently bonding enzymes to the polydopamine (PDA) layer along with the formation of such colloidosomes with lipase as a model enzyme. In this enzyme system, the PDA layer served as a cross-linking layer and enzyme support for simultaneously enhancing the colloidosomes' stability and improving surface availability of the enzymes for catalytic reaction. It was found that the specific activity of lipases immobilized on the colloidosome shells was 8 and 1.4 times higher than that of free lipase and encapsulated lipase positioned in the aqueous cores of colloidosomes, respectively. Moreover, the immobilized lipases demonstrated excellent operational stability and recyclability, retaining 86.6% of enzyme activity after 15 cycles. It is therefore reasonable to expect that this novel approach for enzyme immobilization has great potential to serve as an important technique for the construction of biocatalytic systems.

Encapsulation of enzymes during the creation of an emulsion is a simple and efficient route for enhancing enzyme catalysis in organic media. Herein, we report a capsule with a shell comprising a monolayer of silica Janus particles (JPs) (referred to as a monolayer capsule) and a Pickering emulsion for the encapsulation of enzyme molecules for catalysis purposes in organic media using amphiphilic silica JPs as building blocks. We demonstrate that the JP capsules had a monolayer shell consisting of closely packed silica JPs (270 nm). The capsules were on average 5-50 μm in diameter. The stability of the JP capsules (Pickering emulsion) was investigated with the use of homogeneous silica nanoparticles as a control. The results show that the emulsion stabilized via amphiphilic silica JPs presented no obvious changes in physical appearance after 15 days, indicating the high stability of the emulsions and JP capsules. Furthermore, the lipase from Candida sp. was chosen as a model enzyme for encapsulation within the JP capsules during their formation. The catalytic performance of lipase was evaluated according to the esterification of 1-hexanol with hexanoic acid. It was found that the specific activity of the encapsulated enzymes (28.7 U mL(-1)) was more than 5.6 times higher than that of free enzymes in a biphasic system (5.1 U mL(-1)). The enzyme activity was further increased by varying the volume ratio of water to oil and the JPs loadings. The enzyme-loaded capsule also exhibited high stability during the reaction process and good recyclability. In particular, the jellification of agarose in the JP capsules further enhanced their operating stability. We believe that the monolayer structure of the JP capsules, together with their high stability, rendered the capsules to be ideal enzyme carriers and microreactors for enzyme catalysis in organic media because they created a large interfacial area and had low mass transfer resistance through the monolayer shell.