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

R. C. Deller; B. M. Carter; I. Zampetakis; F. Scarpa; A. W. 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)

R. C. Deller, B. M. Carter, I. Zampetakis, F. Scarpa, A. W. Perriman^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

15 Citations (Scopus)

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
DOIs	https://doi.org/10.1016/j.bbrc.2017.11.073
Publication status	Published - 1 Jan 2018
Externally published	Yes

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10.1016/j.bbrc.2017.11.073

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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, Cryopreservation, Ice recrystallization, Synchrotron radiation circular dichroism, Thermal stability",

author = "Deller, \{R. C.\} and Carter, \{B. M.\} and I. Zampetakis and F. Scarpa and Perriman, \{A. W.\}",

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

AU - Deller, R. C.

AU - Carter, B. M.

AU - Zampetakis, I.

AU - Scarpa, F.

AU - Perriman, A. W.

PY - 2018/1/1

Y1 - 2018/1/1

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.

KW - Antifreeze protein

KW - Cryopreservation

KW - Ice recrystallization

KW - Synchrotron radiation circular dichroism

KW - Thermal stability

UR - https://www.scopus.com/pages/publications/85034967155

U2 - 10.1016/j.bbrc.2017.11.073

DO - 10.1016/j.bbrc.2017.11.073

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C2 - 29137985

AN - SCOPUS:85034967155

SN - 0006-291X

VL - 495

SP - 1055

EP - 1060

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

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

Abstract

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