Probing Protein Kinase (CK2) and Alkaline Phosphatase with CdSe/ZnS Quantum Dots

被引：215

作者：

Freeman, Ronit ^{[1
]}

Finder, Tali ^{[1
]}

Gill, Ron ^{[1
]}

Willner, Itamar ^{[1
]}

机构：

[1] Hebrew Univ Jerusalem, Inst Chem, Ctr Nanosci & Nanotechnol, IL-91904 Jerusalem, Israel

来源：

NANO LETTERS | 2010年 / 10卷 / 06期

关键词：

Quantum dots; casein kinase; CdSe/ZnS; alkaline phosphatase; sensor; RESONANCE ENERGY-TRANSFER; FLUORESCENCE POLARIZATION; GOLD NANOPARTICLES; ASSAY; BIOANALYSIS; GLUCOSE; DONORS;

D O I：

10.1021/nl101052f

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Semiconductor quantum dots (QDs) are used for the optical analysis of casein kinase (CK2) or the hydrolytic activity of alkaline phosphatase (ALP). Two schemes for the analysis of CK2 by a FRET-based mechanism are described. One approach involves the CK2-catalyzed phosphorylation of a serine-containing peptide (1), linked to CdSe/ZnS QDs, with Atto-590-functionalized ATP. The second analytical method involves the specific association of the Atto-590-functionalized antibody to the phosphorylated product. The hydrolytic activity of ALP is followed by the application of phosphotyrosine (4)-modified CdSe/ZnS QDs in the presence of tyrosinase as a secondary reporter biocatalyst. The hydrolysis of (4) yields the tyrosine units that are oxidized by O-2/tyrosinase to the respective dopaquinone product. The latter quinone units quench the QDs via an electron transfer route, leading to the optical detection of the ALP activity.

引用

页码：2192 / 2196

页数：5

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