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Inorg Chem. 2014 Feb 17;53(4):1816-23. doi: 10.1021/ic401612z. Epub 2013 Oct 16.

Peptide tag/probe pairs based on the coordination chemistry for protein labeling.

Author information

1
Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University , Katsura, Kyoto 615-8510, Japan.

Abstract

Protein-labeling methods serve as essential tools for analyzing functions of proteins of interest under complicated biological conditions such as in live cells. These labeling methods are useful not only to fluorescently visualize proteins of interest in biological systems but also to conduct protein and cell analyses by harnessing the unique functions of molecular probes. Among the various labeling methods available, an appropriate binding pair consisting of a short peptide and a de novo designed small molecular probe has attracted attention because of its wide utility and versatility. Interestingly, most peptide tag/probe pairs exploit metal-ligand coordination interactions as the main binding force responsible for their association. Herein, we provide an overview of the recent progress of these coordination-chemistry-based protein-labeling methods and their applications for fluorescence imaging and functional analysis of cellular proteins, while highlighting our originally developed labeling methods. These successful examples clearly exemplify the utility and versatility of metal coordination chemistry in protein functional analysis.

PMID:
24131471
DOI:
10.1021/ic401612z
[Indexed for MEDLINE]

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