Probing protein kinase (CK2) and alkaline phosphatase with CdSe/ZnS quantum dots

Ronit Freeman; Tali Finder; Ron Gill; Itamar Willner

doi:10.1021/nl101052f

Probing protein kinase (CK2) and alkaline phosphatase with CdSe/ZnS quantum dots

Ronit Freeman, Tali Finder, Ron Gill, Itamar Willner^*

^*Corresponding author for this work

Institute of Chemistry

Research output: Contribution to journal › Article › peer-review

232 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	2192-2196
Number of pages	5
Journal	Nano Letters
Volume	10
Issue number	6
DOIs	https://doi.org/10.1021/nl101052f
State	Published - 9 Jun 2010

Keywords

Alkaline phosphatase
Casein kinase
CdSe/ZnS
Quantum dots
Sensor

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10.1021/nl101052f

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title = "Probing protein kinase (CK2) and alkaline phosphatase with CdSe/ZnS quantum dots",

abstract = "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.",

keywords = "Alkaline phosphatase, Casein kinase, CdSe/ZnS, Quantum dots, Sensor",

author = "Ronit Freeman and Tali Finder and Ron Gill and Itamar Willner",

year = "2010",

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doi = "10.1021/nl101052f",

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T1 - Probing protein kinase (CK2) and alkaline phosphatase with CdSe/ZnS quantum dots

AU - Freeman, Ronit

AU - Finder, Tali

AU - Gill, Ron

AU - Willner, Itamar

PY - 2010/6/9

Y1 - 2010/6/9

N2 - 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.

AB - 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.

KW - Alkaline phosphatase

KW - Casein kinase

KW - CdSe/ZnS

KW - Quantum dots

KW - Sensor

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ER -

Probing protein kinase (CK2) and alkaline phosphatase with CdSe/ZnS quantum dots

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