A protein kinase assay based on FRET between quantum dots and fluorescently-labeled peptides

Shujiro Shiosaki; Takanobu Nobori; Takeshi Mori; Riki Toita; Yuta Nakamura; Chan Woo Kim; Tatsuhiro Yamamoto; Takuro Niidome; Yoshiki Katayama

doi:10.1039/c3cc41680a

A protein kinase assay based on FRET between quantum dots and fluorescently-labeled peptides

Shujiro Shiosaki, Takanobu Nobori, Takeshi Mori, Riki Toita, Yuta Nakamura, Chan Woo Kim, Tatsuhiro Yamamoto, Takuro Niidome, Yoshiki Katayama

Materials Science and Engineering, School of Engineering

Research output: Contribution to journal › Article

28 Citations (Scopus)

Abstract

A novel protein kinase assay was developed, based on FRET between QDs and fluorescently-labeled substrate peptides. The negatively charged QDs recognize the change in net charge of the peptide upon phosphorylation. Despite its simple mechanism, this assay is sensitive and robust enough to be applied to the evaluation of protein kinase inhibitors.

Original language	English
Pages (from-to)	5592-5594
Number of pages	3
Journal	Chemical Communications
Volume	49
Issue number	49
DOIs	https://doi.org/10.1039/c3cc41680a
Publication status	Published - May 23 2013

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All Science Journal Classification (ASJC) codes

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
Chemistry(all)
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

Cite this

Shiosaki, S., Nobori, T., Mori, T., Toita, R., Nakamura, Y., Woo Kim, C., ... Katayama, Y. (2013). A protein kinase assay based on FRET between quantum dots and fluorescently-labeled peptides. Chemical Communications, 49(49), 5592-5594. https://doi.org/10.1039/c3cc41680a

A protein kinase assay based on FRET between quantum dots and fluorescently-labeled peptides. / Shiosaki, Shujiro; Nobori, Takanobu; Mori, Takeshi; Toita, Riki; Nakamura, Yuta; Woo Kim, Chan; Yamamoto, Tatsuhiro; Niidome, Takuro; Katayama, Yoshiki.

In: Chemical Communications, Vol. 49, No. 49, 23.05.2013, p. 5592-5594.

Research output: Contribution to journal › Article

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Access to Document

10.1039/c3cc41680a