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

Research output: Contribution to journalReview article

24 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1816-1823
Number of pages8
JournalInorganic Chemistry
Volume53
Issue number4
DOIs
Publication statusPublished - Feb 17 2014

Fingerprint

Labeling
marking
peptides
chemistry
proteins
Peptides
probes
Proteins
functional analysis
Molecular Probes
Functional analysis
versatility
Metals
Biological systems
cells
metals
Fluorescence
Association reactions
Ligands
Imaging techniques

All Science Journal Classification (ASJC) codes

  • Inorganic Chemistry
  • Physical and Theoretical Chemistry

Cite this

Peptide tag/probe pairs based on the coordination chemistry for protein labeling. / Uchinomiya, Shohei; Ojida, Akio; Hamachi, Itaru.

In: Inorganic Chemistry, Vol. 53, No. 4, 17.02.2014, p. 1816-1823.

Research output: Contribution to journalReview article

@article{347b484062ca4b85aa5348832eec37f8,
title = "Peptide tag/probe pairs based on the coordination chemistry for protein labeling",
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.",
author = "Shohei Uchinomiya and Akio Ojida and Itaru Hamachi",
year = "2014",
month = "2",
day = "17",
doi = "10.1021/ic401612z",
language = "English",
volume = "53",
pages = "1816--1823",
journal = "Inorganic Chemistry",
issn = "0020-1669",
publisher = "American Chemical Society",
number = "4",

}

TY - JOUR

T1 - Peptide tag/probe pairs based on the coordination chemistry for protein labeling

AU - Uchinomiya, Shohei

AU - Ojida, Akio

AU - Hamachi, Itaru

PY - 2014/2/17

Y1 - 2014/2/17

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84894295644&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84894295644&partnerID=8YFLogxK

U2 - 10.1021/ic401612z

DO - 10.1021/ic401612z

M3 - Review article

VL - 53

SP - 1816

EP - 1823

JO - Inorganic Chemistry

JF - Inorganic Chemistry

SN - 0020-1669

IS - 4

ER -