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

doi:10.1016/j.bbrc.2017.11.073

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 journal › Article (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 language	English
Pages (from-to)	1055-1060
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	495
Issue number	1
Early online date	11 Nov 2017
DOIs	https://doi.org/10.1016/j.bbrc.2017.11.073
Publication status	Published - 1 Jan 2018

Keywords

Antifreeze protein
Synchrotron radiation circular dichroism
Ice recrystallization
Thermal stability
Cryopreservation

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10.1016/j.bbrc.2017.11.073

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Functional Biomolecular Liquids
Perriman, A. W.
1/10/13 → 30/09/18
Project: Research

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

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.",

keywords = "Antifreeze protein, Synchrotron radiation circular dichroism, Ice recrystallization, Thermal stability, Cryopreservation",

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The effect of surface charge on the thermal stability and ice recrystallization inhibition activity of antifreeze protein III (AFP III). / Deller, Robert; Carter, Ben; Zampetakis, Ioannis; Scarpa, Fabrizio ; Perriman, Adam.

In: Biochemical and Biophysical Research Communications, Vol. 495, No. 1, 01.01.2018, p. 1055-1060.

Research output: Contribution to journal › Article (Academic Journal) › peer-review

TY - JOUR

T1 - The effect of surface charge on the thermal stability and ice recrystallization inhibition activity of antifreeze protein III (AFP III)

AU - Deller, Robert

AU - Carter, Ben

AU - Zampetakis, Ioannis

AU - Scarpa, Fabrizio

AU - Perriman, Adam

PY - 2018/1/1

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N2 - 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.

AB - 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.

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KW - Synchrotron radiation circular dichroism

KW - Ice recrystallization

KW - Thermal stability

KW - Cryopreservation

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

Abstract

Keywords

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Functional Biomolecular Liquids

Cite this