Ice-binding proteins and the applicability and limitations of the kinetic pinning model.

Ice-binding proteins (IBPs) are unique molecules that bind to and are active on the interface between two phases of water: ice and liquid water. This property allows them to affect ice growth in multiple ways: shaping ice crystals, suppressing the freezing point, inhibiting recrystallization and promoting nucleation. Advances in the protein's production technologies make these proteins promising agents for medical applications among others. Here, we focus on a special class of IBPs that suppress freezing by causing thermal hysteresis (TH): antifreeze proteins (AFPs). The kinetic pinning model describes the dynamics of a growing ice face with proteins binding to it, which eventually slow it down to a halt. We use the kinetic pinning model, with some adjustments made, to study the TH dependence on the solution's concentration of AFPs by fitting the model to published experimental data. We find this model describes the activity of (moderate) type III AFPs well, but is inadequate for the (hyperactive) Tenebrio molitor AFPs. We also find the engulfment resistance to be a key parameter, which depends on the protein's size. Finally, we explain intuitively how TH depends on the seeding time of the ice crystal in the protein solution. Using this insight, we explain the discrepancy in TH measurements between different assays. This article is part of the theme issue 'The physics and chemistry of ice: scaffolding across scales, from the viability of life to the formation of planets'.

Broadband surface plasmon wave excitation using dispersion engineering.

High sensitivity of surface-plasmon-based sensors stems from the fact that the surface plasmon is a resonance phenomenon. The resonance results from the phase-matching condition when the phase velocity of the surface plasmon wave and of the lateral component of the incident light become equal. We show that this condition can be satisfied simultaneously for many wavelengths. We demonstrate numerically and experimentally that this allows a surface plasmon resonance that extends over a broad wavelength range. We consider two methods of excitation of such broadband surface plasmon resonance: (i) patterning the interface where the surface plasmon propagates and (ii) broadband coupling through dispersion compensation. We demonstrate extremely broadband surface plasmon excitation at the Au-water or Au-air interface that extends through the whole near-infrared range from λ = 1 µm to 3 µm. We show how this broadband surface plasmon can be used for sensitive spectroscopic sensing, in particular for monitoring wetting/dewetting processes such as thin liquid film growth.

Male-female communication enhances release of extracellular vesicles leading to high fertility in Drosophila.

The female reproductive tract (female-RT) must decipher the repertoire of molecular cues received from the male during copulation in order to activate and coordinate tract functionality necessary for high fertility. In Drosophila, this modulation is partially driven by spermathecal secretory cells (SSC). The SSC are a layer of cuboidal secretory glandular cells surrounding the spermatheca capsule where sperm is stored. It is unclear, however, how the SSC regulate the system's activity. Here we show that mating activates the secretory machinery of the SSC. The SSC release a heterogeneous population of extracellular vesicles (EVs) which is involved in initiating and managing the increase in egg-laying, and possibly sperm storage. Moreover, sperm and male accessory gland proteins are essential for such mating-mediated SSC activity. Thus, mating regulates secretory/endocytic pathways required for trafficking of vesicles to SSC-female-RT target sites, which modulate and coordinate reproductive tract activity to achieve high fertility.

Cellulose Nanocrystals and Corn Zein Oxygen and Water Vapor Barrier Biocomposite Films.

Cellulose nanocrystals (CNC) are well-suited to the preparation of biocomposite films and packaging material due to its abundance, renewability, biodegradability, and favorable film-forming capacity. In this study, different CNC and corn zein (CZ) composite films were prepared by adding CZ to the CNC suspension prior to drying, in order to change internal structure of resulting films. Films were developed to examine their performance as an alternative water vapor and oxygen-barrier for flexible packaging industry. Water vapor permeability (WVP) and oxygen transmission rate (OTR) of the biocomposite films decreased significantly in a specific ratio between CNC and CZ combined with 1,2,3,4-butane tetracarboxylic acid (BTCA), a nontoxic cross linker. In addition to the improved barrier properties, the incorporation of CZ benefitted the flexibility and thermal stability of the CNC/CZ composite films. The toughness increased by 358%, and Young's modulus decreased by 32% compared with the pristine CNC film. The maximum degradation temperature increased by 26 °C, compared with that of CNC film. These results can be attributed to the incorporation of a hydrophobic protein into the matrix creating hydrophobic interactions among the biocomposite components. SEM and AFM analysis indicated that CZ could significantly affect the CNC arrangement, and the film surface topography, due to the mechanical bundling and physical adsorption effect of CZ to CNC. The presented results indicate that CNC/CZ biocomposite films may find applications in packaging, and in multi-functionalization materials.

Ice Nucleation Properties of Ice-binding Proteins from Snow Fleas.

Ice-binding proteins (IBPs) are found in many organisms, such as fish and hexapods, plants, and bacteria that need to cope with low temperatures. Ice nucleation and thermal hysteresis are two attributes of IBPs. While ice nucleation is promoted by large proteins, known as ice nucleating proteins, the smaller IBPs, referred to as antifreeze proteins (AFPs), inhibit the growth of ice crystals by up to several degrees below the melting point, resulting in a thermal hysteresis (TH) gap between melting and ice growth. Recently, we showed that the nucleation capacity of two types of IBPs corresponds to their size, in agreement with classical nucleation theory. Here, we expand this finding to additional IBPs that we isolated from snow fleas (the arthropod Collembola), collected in northern Israel. Chemical analyses using circular dichroism and Fourier-transform infrared spectroscopy data suggest that these IBPs have a similar structure to a previously reported snow flea antifreeze protein. Further experiments reveal that the ice-shell purified proteins have hyperactive antifreeze properties, as determined by nanoliter osmometry, and also exhibit low ice-nucleation activity in accordance with their size.