Effect of Graphene Composite on Biological Egg Protein Resistance Switching Memory Properties

In this work, a resistive switching memory device was fabricated based on egg protein, a natural biomaterial. The effect of graphene composite on the resistive switching characteristics of the device was investigated. The experimental results show that both pure egg protein and graphene composite devices exhibit bipolar nonvolatile resistive conversion properties. Both devices have good data retention capability. Furthermore, the composite of graphene can effectively improve the device endurance and the consistency of the on-state current distribution of the device. Based on the theory of capture and de-capture of charge carrier, the mechanism of resistive switching is analyzed.

Bacillus thuringiensis chimeric proteins Cry1A.2 and Cry1B.2 to control soybean lepidopteran pests: New domain combinations enhance insecticidal spectrum of activity and novel receptor contributions

Two new chimeric Bacillus thuringiensis (Bt) proteins, Cry1A.2 and Cry1B.2, were constructed using specific domains, which provide insecticidal activity against key lepidopteran soybean pests while minimizing receptor overlaps between themselves, current, and soon to be commercialized plant incorporated protectants (PIP’s) in soybean. Results from insect diet bioassays demonstrate that the recombinant Cry1A.2 and Cry1B.2 are toxic to soybean looper (SBL) Chrysodeixis includens Walker, velvetbean caterpillar (VBC) Anticarsia gemmatalis Hubner, southern armyworm (SAW) Spodoptera eridania, and black armyworm (BLAW) Spodoptera cosmioides with LC50 values < 3,448 ng/cm2. Cry1B.2 is of moderate activity with significant mortality and stunting at > 3,448 ng/cm2, while Cry1A.2 lacks toxicity against old-world bollworm (OWB) Helicoverpa armigera. Results from disabled insecticidal protein (DIP) bioassays suggest that receptor utilization of Cry1A.2 and Cry1B.2 proteins are distinct from each other and from current, and yet to be commercially available, Bt proteins in soy such as Cry1Ac, Cry1A.105, Cry1F.842, Cry2Ab2 and Vip3A. However, as Cry1A.2 contains a domain common to at least one commercial soybean Bt protein, resistance to this common domain in a current commercial soybean Bt protein could possibly confer at least partial cross resistance to Cry1A2. Therefore, Cry1A.2 and Cry1B.2 should provide two new tools for controlling many of the major soybean insect pests described above.

Preparation and Performance of Silica-di-Block Polymer Hybrids for BSA-Resistance Coatings

A series of tem-responsive and protein-resistance property silica-di-block polymers SiO2-g-PMMA-b-P(PEGMA) hybrids are synthesized with methyl methacrylate (MMA) and poly (ethylene glycol) methyl ether methacrylate (PEGMA) by the surface-initiated atom transfer radical polymerization (SI-ATRP). The morphology in tetrahydrofuran (THF) solution, lower critical solution temperature (LCST), surface morphology, bovine serum albumin (BSA)-resistance property, and thermal stability of nanoparticles were analyzed. The results of 1H-NMR, GPC, and TEM prove that the silica-di-block hybrids have been obtained. The silica-di-block hybrids shows the LCST (52–64 °C) in aqueous solution. The hybrid films casted by THF present distributed uniform granular bulges and the film surface is relatively smooth (Ra = 15.4 nm ~ 10.5 nm). The results of QCM-D showed that only a small amount of BSA protein(△f = 18.6 ~ 11.8 Hz) was adsorbed on the surface of the films. The result of XPS also demonstrated that only a small amount of BSA protein was absorbed onto the surface of the film (N% = 1.86). The TGA analyses indicate that the thermal decomposition temperature of hybrids is 288 °C. Thus, it is suggested that the hybrids are served as a suitable coating with BSA resistance property and thermal stability.

The development of an antifouling interpenetrating polymer network hydrogel film for salivary glucose monitoring

A stable hydration layer is formed in an IPN hydrogel that can achieve high protein resistance and high glucose sensitivity.

Nanoscale in silico classification of ligand functionalised surfaces for protein adsorption resistance

Non-specific protein adsorption represents a challenge for the design of efficient and safe nanoparticles for biomedical applications. An in silico method is presented to design ligands imparting protein resistance to functional surfaces.