Ice nucleation properties of ice-binding proteins from snow fleas

Akalabya Bissoyi, Naama Reicher, Michael Chasnitsky, Sivan Arad, Thomas Koop, Yinon Rudich, Ido Braslavsky*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


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.

Original languageAmerican English
Article number532
Issue number10
StatePublished - Oct 2019

Bibliographical note

Publisher Copyright:
© 2019 by the authors. Licensee MDPI, Basel, Switzerland.


  • Antifreeze proteins
  • Collembola in Israel
  • Hyperactive
  • Hypogastruridae
  • Ice binding proteins
  • Ice nucleation
  • Thermal hysteresis


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