Microfluidic experiments reveal that antifreeze proteins bound to ice crystals suffice to prevent their growth

Yeliz Celik, Ran Drori, Natalya Pertaya-Braun, Aysun Altan, Tyler Barton, Maya Bar-Dolev, Alex Groisman, Peter L. Davies, Ido Braslavsky*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

136 Scopus citations

Abstract

Antifreeze proteins (AFPs) are a subset of ice-binding proteins that control ice crystal growth. They have potential for the cryopreservation of cells, tissues, and organs, as well as for production and storage of food and protection of crops from frost. However, the detailed mechanism of action of AFPs is still unclear. Specifically, there is controversy regarding reversibility of binding of AFPs to crystal surfaces. The experimentally observed dependence of activity ofAFPs ontheir concentration in solution appears to indicate that the binding is reversible. Here, by a series of experiments in temperature- controlledmicrofluidic devices, where the medium surrounding ice crystals can be exchanged, we show that the binding of hyperactive Tenebriomolitor AFP to ice crystals is practically irreversible and that surface-bound AFPs are sufficient to inhibit ice crystal growth even in solutions depleted of AFPs. These findings rule out theories of AFP activity relying on the presence of unbound protein molecules.

Original languageAmerican English
Pages (from-to)1309-1314
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume110
Issue number4
DOIs
StatePublished - 22 Jan 2013

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