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

8 Citations (Scopus)

308 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

Access to Document

10.1016/j.bbrc.2017.11.073

Full-text PDF (accepted author manuscript)
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, 3.39 MB

Cite this

@article{911a849053c54478a97e15ca29db6255,

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",

author = "Robert Deller and Ben Carter and Ioannis Zampetakis and Fabrizio Scarpa and Adam Perriman",

year = "2018",

month = jan,

day = "1",

doi = "10.1016/j.bbrc.2017.11.073",

language = "English",

volume = "495",

pages = "1055--1060",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press",

number = "1",

}

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

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 - Synchrotron radiation circular dichroism

KW - Ice recrystallization

KW - Thermal stability

KW - Cryopreservation

UR - http://www.scopus.com/inward/record.url?scp=85034967155&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2017.11.073

DO - 10.1016/j.bbrc.2017.11.073

M3 - Article (Academic Journal)

C2 - 29137985

AN - SCOPUS:85034967155

VL - 495

SP - 1055

EP - 1060

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -

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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Functional Biomolecular Liquids

Cite this

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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Projects

Functional Biomolecular Liquids

Cite this