The effect of surface charge on the thermal stability and ice recrystallization inhibition activity of antifreeze protein III (AFP III)

Robert Deller, Ben Carter, Ioannis Zampetakis, Fabrizio Scarpa, Adam Perriman*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

6 Citations (Scopus)
301 Downloads (Pure)

Abstract

The aim of this study was to examine the effect of chemical cationization on the structure and function of antifreeze protein III (AFP III) over an extreme temperature range (−40°C to +90°C) using far-UV synchrotron radiation circular dichroism (SRCD) and ice recrystallization inhibition (IRI) assays. Chemical cationization was able to produce a modified AFP III with a net cationic charge at physiological pH that had enhanced resistance to denaturation at elevated temperatures, with no immediate negative impact on protein structure at subzero temperatures. Furthermore, cationized AFP III retained an IRI activity similar to that of native AFP III. Consequently, chemical cationization may provide a pathway to the development of more robust antifreeze proteins as supplementary cryoprotectants in the cryopreservation of clinically relevant cells.

Original languageEnglish
Pages (from-to)1055-1060
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume495
Issue number1
Early online date11 Nov 2017
DOIs
Publication statusPublished - 1 Jan 2018

Keywords

  • Antifreeze protein
  • Synchrotron radiation circular dichroism
  • Ice recrystallization
  • Thermal stability
  • Cryopreservation

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