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

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)1055-1060
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume495
Issue number1
Early online date11 Nov 2017
DOIs
DateAccepted/In press - 10 Nov 2017
DateE-pub ahead of print - 11 Nov 2017
DatePublished (current) - 1 Jan 2018

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.

    Research areas

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

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  • Full-text PDF (accepted author manuscript)

    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via Elsevier at https://www.sciencedirect.com/science/article/pii/S0006291X17322519#!. Please refer to any applicable terms of use of the publisher.

    Accepted author manuscript, 3 MB, PDF-document

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