Analysis of antifreeze protein activity using colorimetric gold nanosensors

Citations

SCOPUS

0

초록

High activity and long stability of antifreeze proteins (AFPs), also known as ice-binding proteins (IBPs), are necessary for exerting their physiological functions in biotechnology and cryomedicine. Here we report a simple analysis of antifreeze protein activity and stability based on self-Assembly of gold nanoparticles (AuNPs) via freezing and thawing cycles. While the mercaptosuccinic acid-capped AuNP (MSA-AuNP) was easily self-Assembled after a freezing/thawing cycle, due to the mechanical attack of ice crystal on the MSA-AuNP surface, the presence of AFP impeded the self-Assembly of MSA-AuNP via the interaction of AFP with ice crystals via freezing and thawing cycles, which led to a strong color in the MSA-AuNP solution. As a result, the aggregation parameter (E520/E650) of MSA-AuNP showed the rapid detection of both activity and stability of AFPs. We suggest that our newly developed method is very suitable for measuring antifreeze activity and stability in a simple and rapid manner with reliable quantification.

키워드

antifreeze protein; colorimetric analysis; gold nanoparticle; ice-binding protein; protein activity; Color; Colorimetric analysis; Colorimetry; Freezing; Gold; Ice; Metal nanoparticles; Nanoparticles; Self assembly; Stability; Thawing; Antifreeze activities; Antifreeze protein; Freezing and thawing cycle; Gold Nanoparticles; Ice binding proteins; Mercaptosuccinic acids; Physiological functions; Protein activity; Proteins
제목
Analysis of antifreeze protein activity using colorimetric gold nanosensors
저자
Jing, Xu; Choi, Ho-seok; Park, Ji-In; Kim, Young-Pil
DOI
10.1117/12.2189039
발행일
2015-07
유형
Conference Paper
저널명
Progress in Biomedical Optics and Imaging - Proceedings of SPIE
권
9523