期刊
SENSORS
卷 15, 期 8, 页码 17977-17989出版社
MDPI AG
DOI: 10.3390/s150817977
关键词
FRET; quantum dot; zinc; kinase; phosphorylation
资金
- Mid-career Researcher Program through National Research Foundation (NRF) - Ministry of Science, ICT, and Future Planning (MSIP) [2013R1A2A2A03015161]
- Nano-Material Technology Development Program through National Research Foundation (NRF) - Ministry of Science, ICT, and Future Planning (MSIP) [2012M3A7B4035286]
- Next-Generation BioGreen 21 Program (SSAC), Rural Development Administration, Korea [PJ01114901]
- National Research Foundation of Korea [22A20130012056, 2012M3A7B4035287, 2013R1A2A2A03015161] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
We report a simple detection of protein kinase activity using Zn(II)-mediated fluorescent resonance energy transfer (FRET) between quantum dots (QDs) and dye-tethered peptides. With neither complex chemical ligands nor surface modification of QDs, Zn(II) was the only metal ion that enabled the phosphorylated peptides to be strongly attached on the carboxyl groups of the QD surface via metal coordination, thus leading to a significant FRET efficiency. As a result, protein kinase activity in intermixed solution was efficiently detected by QD-FRET via Zn(II) coordination, especially when the peptide substrate was combined with affinity-based purification. We also found that mono- and di-phosphorylation in the peptide substrate could be discriminated by the Zn(II)-mediated QD-FRET. Our approach is expected to find applications for studying physiological function and signal transduction with respect to protein kinase activity.
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