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Discussion papers
https://doi.org/10.5194/acp-2019-861
© Author(s) 2019. This work is distributed under
the Creative Commons Attribution 4.0 License.
https://doi.org/10.5194/acp-2019-861
© Author(s) 2019. This work is distributed under
the Creative Commons Attribution 4.0 License.

Submitted as: research article 07 Oct 2019

Submitted as: research article | 07 Oct 2019

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This discussion paper is a preprint. It is a manuscript under review for the journal Atmospheric Chemistry and Physics (ACP).

Protein aggregates nucleate ice: the example of apoferritin

María Cascajo-Castresana1,2,3, Robert O. David3,4, Maiara A. Iriarte-Alonso2, Alexander M. Bittner2,5, and Claudia Marcolli3 María Cascajo-Castresana et al.
  • 1División de Salud, TECNALIA, Parque Tecnológico, Paseo de Mikeletegi, 2, 20009 Donostia, Spain
  • 2CIC nanoGUNE, Tolosa Hiribidea, 76, 20018 Donostia, Spain
  • 3Department of Environmental System Sciences, Institute for Atmospheric and Climate Science, ETH Zurich, 8092 Zurich, Switzerland
  • 4Department of Geosciences, University of Oslo, Oslo, 0315, Norway
  • 5Ikerbasque, Basque Foundation for Science, Ma Díaz de Haro 3, 48013 Bilbao, Spain

Abstract. 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 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.

María Cascajo-Castresana et al.
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Short summary
Atmospheric ice-nucleating particles are rare but relevant for cloud glaciation. A source of particles that nucleate ice above −15 °C is biological material including some proteins. Here we show that proteins of very diverse functions and structures can nucleate ice. Among these, the iron storage protein apoferritin stands out, with activity up to −4 °C. We show that its activity does not stem from correctly assembled proteins but from misfolded protein monomers or oligomers and aggregates.
Atmospheric ice-nucleating particles are rare but relevant for cloud glaciation. A source of...
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