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Frozen assembly of gold nanoparticles for rapid analysis of antifreeze protein activity

Cited 9 time in wos
Cited 10 time in scopus
Title
Frozen assembly of gold nanoparticles for rapid analysis of antifreeze protein activity
Other Titles
금 나노 입자의 동결응집 반응을 이용한 결빙방지단백질의 활성 측정 방법 개발
Authors
Park, Ji-In
Lee, Jun Hyuck
Gwak, Yunho
Kim, Hak Jun
Jin, EonSeon
Kim, Young-Pil
Subject
BiophysicsBiotechnology & Applied MicrobiologyChemistryElectrochemistryScience & Technology - Other Topics
Keywords
Antifreeze proteinFrozen assemblyGold nanoparticleIce-binding proteinThermal hysteresis
Issue Date
2013-03-15
Citation
Park, Ji-In, et al. 2013. "Frozen assembly of gold nanoparticles for rapid analysis of antifreeze protein activity". Biosensors and Bioelectronics, 41(1): 752-757.
Abstract
We report the novel activity-based detection of antifreeze protein (APP), also known as ice-binding protein (IBP), using freeze-labile gold nanoparticles (AuNPs) in order to overcome labor-intensive and low throughput issues of the current method based on thermal hysteresis (TH). Upon the addition of either CnAFP from the Antarctic diatom Chaetoceros neogracile or LeIBP from the Arctic yeast Leucosporidium sp. to mercaptosuccinic acid-capped AuNP, the self-assembly of AuNPs was highly inhibited after a freezing/thawing cycle, leading to no color change in the AuNP solution. As a result, the aggregation parameter (E-520/E-650) of AuNP presented the rapid detection of both the concentration-dependent activity and stability of two AFPs with high sensitivity, where the detection range was 100-fold lower than that of the TH-based method. We suggest that our newly developed method is very suitable for simple and high-throughput measurement of AFP activity. (C) 2012 Elsevier B.V. All rights reserved.
URI
https://repository.kopri.re.kr/handle/201206/13035
DOI
http://dx.doi.org/10.1016/j.bios.2012.09.052
Type
Article
Indexed
SCI
Appears in Collections  
2011 Polar Academic Program (PD11010)
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