TY - JOUR
T1 - Design of a binuclear Ni(II)-iminodiacetic acid (IDA) complex for selective recognition and covalent labeling of His-tag fused proteins
AU - Takahira, Ikuko
AU - Fuchida, Hirokazu
AU - Tabata, Shigekazu
AU - Shindo, Naoya
AU - Uchinomiya, Shohei
AU - Hamachi, Itaru
AU - Ojida, Akio
N1 - Funding Information:
We appreciate the technical support from the Research Support Center, Graduate School of Medical Sciences, Kyushu University. This work was performed under the Cooperative Research Program of ‘Network Joint Research Center for Materials and Devices’. A.O. acknowledges Takeda Science Foundation and Toray Science Foundation for their financial supports. S.T. acknowledges Kyushu University Interdisciplinary Programs in Education and Projects in Research Development for its financial support.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 2014/7/1
Y1 - 2014/7/1
N2 - Selective protein labeling with a small molecular probe is a versatile method for elucidating protein functions under live-cell conditions. In this Letter, we report the design of the binuclear Ni(II)-iminodiacetic acid (IDA) complex for selective recognition and covalent labeling of His-tag-fused proteins. We found that the Ni(II)-IDA complex 1-2Ni(II) binds to the His6-tag (HHHHHH) with a strong binding affinity (Kd = 24 nM), the value of which is 16-fold higher than the conventional Ni(II)-NTA complex (Kd = 390 nM). The strong binding affinity of the Ni(II)-IDA complex was successfully used in the covalent labeling and fluorescence bioimaging of a His-tag fused GPCR (G-protein coupled receptor) located on the surface of living cells.
AB - Selective protein labeling with a small molecular probe is a versatile method for elucidating protein functions under live-cell conditions. In this Letter, we report the design of the binuclear Ni(II)-iminodiacetic acid (IDA) complex for selective recognition and covalent labeling of His-tag-fused proteins. We found that the Ni(II)-IDA complex 1-2Ni(II) binds to the His6-tag (HHHHHH) with a strong binding affinity (Kd = 24 nM), the value of which is 16-fold higher than the conventional Ni(II)-NTA complex (Kd = 390 nM). The strong binding affinity of the Ni(II)-IDA complex was successfully used in the covalent labeling and fluorescence bioimaging of a His-tag fused GPCR (G-protein coupled receptor) located on the surface of living cells.
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U2 - 10.1016/j.bmcl.2014.04.096
DO - 10.1016/j.bmcl.2014.04.096
M3 - Article
C2 - 24835629
AN - SCOPUS:84901786542
SN - 0960-894X
VL - 24
SP - 2855
EP - 2858
JO - Bioorganic and Medicinal Chemistry Letters
JF - Bioorganic and Medicinal Chemistry Letters
IS - 13
ER -