期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 495, 期 1, 页码 1055-1060出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2017.11.073
关键词
Antifreeze protein; Synchrotron radiation circular dichroism; Ice recrystallization; Thermal stability; Cryopreservation
资金
- EPSRC [EP/K026720/1]
- EPSRC [EP/K026720/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [EP/K026720/1] Funding Source: researchfish
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 degrees C to +90 degrees 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. (C) 2017 Published by Elsevier Inc.
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