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Biological material has gained increasing attention recently as a source of ice-nucleating particles that may account for cloud glaciation at moderate supercooling. While the ice-nucleation (IN) ability of some bacteria can be related to membrane-bound proteins with epitaxial fit to ice, little is known about the IN-active entities present in biological material in general. To elucidate the potential of proteins and viruses to contribute to the IN activity of biological material, we performed bulk freezing experiments with the newly developed drop freezing assay DRoplet Ice Nuclei Counter Zurich (DRINCZ), which allows the simultaneous cooling of 96 sample aliquots in a chilled ethanol bath. We performed a screening of common proteins, namely the iron storage protein ferritin and its iron-free counterpart apoferritin, the milk protein casein, the egg protein ovalbumin, two hydrophobins, and a yeast ice-binding protein, all of which revealed IN activity with active site densities > 0.1 mg−1 at −10 ∘C. The tobacco mosaic virus, a plant virus based on helically assembled proteins, also proved to be IN active with active site densities increasing from 100 mg−1 at −14 ∘C to 10 000 mg−1 at −20 ∘C. Among the screened proteins, the IN activity of horse spleen ferritin and apoferritin, which form cages of 24 co-assembled protein subunits, proved to be outstanding with active site densities > 10 mg−1 at −5 ∘C. Investigation of the pH dependence and heat resistance of the apoferritin sample confirmed the proteinaceous nature of its IN-active entities but excluded the correctly folded cage monomer as the IN-active species. A dilution series of apoferritin in water revealed two distinct freezing ranges, an upper one from −4 to −11 ∘C and a lower one from −11 to −21 ∘C. Dynamic light scattering measurements related the upper freezing range to ice-nucleating sites residing on aggregates and the lower freezing range to sites located on misfolded cage monomers or oligomers. The sites proved to persist during several freeze–thaw cycles performed with the same sample aliquots. Based on these results, IN activity seems to be a common feature of diverse proteins, irrespective of their function, but arising only rarely, most probably through defective folding or aggregation to structures that are IN active.

In patients with comorbidities, a large number of wounds become chronic, representing an overwhelming economic burden for healthcare systems. Engineering the microenvironment is a paramount trend to activate cells and burst-healing mechanisms. The extrusion bioprinting of advanced dressings was performed with novel composite bioinks made by blending adipose decellularized extracellular matrix with plasma and human dermal fibroblasts. Rheological and microstructural assessments of the composite hydrogels supported post-printing cell viability and proliferation over time. Embedded fibroblasts expressed steady concentrations of extracellular matrix proteins, including type 1, 3 and 4 collagens and fibronectin. ELISA assessments, multiplex protein arrays and ensuing bioinformatic analyses revealed paracrine activities corresponding to wound-healing activation through the modulation of inflammation and angiogenesis. The two modalities of advanced dressings, differing in platelet number, showed differences in the release of inflammatory and angiogenic cytokines, including interleukin 8 (IL-8), monocyte chemotactic protein 1 (MCP-1), vascular endothelial growth factor (VEGF) and hepatocyte growth factor (HGF). The conditioned media stimulated human-dermal-cell proliferation over time. Our findings open the door to engineering the microenvironment as a strategy to enhance healing.

We employed environmental scanning electron microscopy (ESEM) in low-humidity atmosphere to study the ice growth, coalescence of crystallites, polycrystalline film morphology, and sublimation, in the temperature range of −10 to −20 ∘C. First, individual ice crystals grow in the shape of micron-sized hexagonal columns with stable basal faces. Their coalescence during further growth results in substantial surface defects and forms thick polycrystalline films, consisting of large grains separated by grain boundaries. The latter are composed of 1 to 3 µm wide pores, which are attributed to the coalescence of defective crystallite surfaces. Sublimation of isolated crystals and of films is defect-driven, and grain boundaries play a decisive role. A scallop-like concave structure forms, limited by sharp ridges, which are terminated by nanoscale asperities. The motivation for this work is also to evaluate ESEM's ability to provide a clean and reproducible environment for future study of nucleation and growth on atmospherically relevant nucleators such as materials of biological origin and inorganic materials. Hence, extensive information regarding potential ESEM beam damage and effect of impurities are discussed.

Ice formation in the atmosphere is important for regulating cloud lifetime, Earth's radiative balance and initiating precipitation. Due to the difference in the saturation vapor pressure over ice and water, in mixed-phase clouds (MPCs), ice will grow at the expense of supercooled cloud droplets. As such, MPCs, which contain both supercooled liquid and ice, are particularly susceptible to ice formation. However, measuring and quantifying the concentration of ice-nucleating particles (INPs) responsible for ice formation at temperatures associated with MPCs is challenging due to their very low concentrations in the atmosphere (∼1 in 105 at −30 ∘C). Atmospheric INP concentrations vary over several orders of magnitude at a single temperature and strongly increase as temperature approaches the homogeneous freezing threshold of water. To further quantify the INP concentration in nature and perform systematic laboratory studies to increase the understanding of the properties responsible for ice nucleation, a new drop-freezing instrument, the DRoplet Ice Nuclei Counter Zurich), is developed. The instrument is based on the design of previous drop-freezing assays and uses a USB camera to automatically detect freezing in a 96-well tray cooled in an ethanol chilled bath with a user-friendly and fully automated analysis procedure. Based on an in-depth characterization of DRINCZ, we develop a new method for quantifying and correcting temperature biases across drop-freezing assays. DRINCZ is further validated performing NX-illite experiments, which compare well with the literature. The temperature uncertainty in DRINCZ was determined to be ±0.9 ∘C. Furthermore, we demonstrate the applicability of DRINCZ by measuring and analyzing field-collected snow samples during an evolving synoptic situation in the Austrian Alps. The field samples fall within previously observed ranges for cumulative INP concentrations and show a dependence on air mass origin and upstream precipitation amount.