Metal‐Chelating Amino Acids as Building Blocks for Synthetic Receptors Sensing Metal Ions and Histidine‐Tagged Proteins.

Hutschenreiter, Silke; Neumann, Lars; Raedler, Ulf; Schmitt, Lutz; Tampé, Robert

doi:10.1002/chin.200409180

Cited by 4 publications

(8 citation statements)

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“…(7) Piehler et al has further studied the enhanced affinity of multivalent Ni-NTA-derived molecules toward the histidine tag in great detail. (8,9,10) In the present work, we wish to design a superparamagnetic iron oxide immobilized bivalent Ni-NTA chelate system with the aim of improving IMAC purification of His×6-tagged proteins by strengthening the interactions between the His×6-tag and the bivalent Ni-NTA chelate. The bis-Ni-NTA-immobilized nanoparticles were shown to be capable of binding His×6-tagged proteins in their native, folded conformations that failed to bind commercial microbeads under identical conditions.…”

Section: Introductionmentioning

confidence: 99%

Highly-Efficient Purification of Native Polyhistidine-Tagged Proteins by Multivalent NTA-Modified Magnetic Nanoparticles

et al. 2007

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A new bis-nitrilotriacetic acid (NTA) chelate with catechol anchor was synthesized and immobilized on superparamagnetic iron oxide nanoparticles. When loaded with Ni(II), these bis-NTA-immobilized nanoparticles were shown to bind polyhistidine (His x 6-tagged) fusion proteins in their native, folded conformations that commercial microbeads failed to bind under identical conditions. Control experiments with a mono-NTA chelate immobilized on iron oxide nanoparticles indicate a similarly high affinity for His x 6-tagged native proteins, suggesting that the high density of the mono-NTA chelate presented by the nanoparticles allows the binding of the His x 6-tag to more than one Ni-NTA moiety on the surface. This study shows that the multivalency strategy can be utilized to enhance the binding of His x 6-tagged proteins in their native, folded conformations. We further demonstrated the selective purification of His x 6-tagged proteins from crude cell lysates by using the Ni(II)-loaded iron oxide nanoparticles. The present platform is capable of efficient purification of His x 6-tagged proteins that are expressed at low levels in mammalian cells. This work thus presents a novel nanoparticle-based high-capacity protein purification system with shorter incubation times, proportionally large washes, and significantly smaller elution volumes compared to commercially available microbeads.

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Section: Introductionmentioning

confidence: 99%

Highly-Efficient Purification of Native Polyhistidine-Tagged Proteins by Multivalent NTA-Modified Magnetic Nanoparticles

et al. 2007

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“…The apparent K d value of ~ 70 µM obtained by ITC for the NTA-Ni 2+ -N-acetylhexahistidine ternary complex ( [43] indicating that in these complexes NTA binds Ni 2+ in a tridentate mode (Fig. 1).…”

Section: Itc Parameters Of N-acetyloligohistidine Sequences Binding Tmentioning

confidence: 94%

“…The importance of this study lies in the potential use of these complexes as tools to create probes for protein labeling and to design novel strategies for bio-imaging of target proteins. [43,56] To investigate the possibility of ternary complex formation between N-acetyloligohistidines and other metal cations-NTA complexes, ITC experiments using NTA complexes of several bivalent metal cations (i.e. Mg 2+ , Ca 2+ , Mn 2+ , Zn 2+ and Co 2+ ), the most commonly found metal ions in living cells, were performed under conditions identical to those employed with Cu 2+ -and Ni 2+ -NTA.…”

Section: Itc Parameters Of N-acetyloligohistidine Sequences Binding Tmentioning

confidence: 99%

“…[36] In addition to the purification of recombinant proteins, the His-tag binding system has been used in membrane separation of recombinant proteins, [37] immobilization of recombinant proteins on interfaces [38,39] and on nanoparticles. [40][41][42] Other applications include the development of biosensors through self-assembly in solution phase [43] of hexahistidine tags with molecules containing two [44][45][46] or three [47][48][49][50] aminocarboxylate residues.…”

Section: Introductionmentioning

confidence: 99%

“…The lack of NTA displacement is evident from the extensive use of NTA-Ni 2+ on interfaces[47,48,73] where the presence of large excess of hexahistidine-tagged proteins does not result in the displacement of NTA by hexahistidine ligands with subsequent leaching of Ni 2+ from interfaces into the solution phase. In homogeneous solutions, titration of analogous Ni 2+ -iminodiacetate derivatized complex by hexahistidine-tagged proteins[43] revealed no displacement of iminodiacetate. Thus, it is reasonable to assume that the species present in appreciable amounts in solutions containing NiSO 4 , at least 1 eq.…”

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confidence: 99%

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Calorimetric studies of ternary complexes of Ni(II) and Cu(II) nitrilotriacetic acid and N-acetyloligohistidines

Mehlenbacher

Bou-Abdallah

Liu

et al. 2015

Inorganica Chimica Acta

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The thermodynamics of Cu 2+-and Ni 2+-NTA binding to polypeptides containing 2-6 histidine residues in neutral buffered aqueous solutions were characterized by isothermal titration calorimetry (ITC). The apparent dissociation constants of ternary complexes of N-acetylhexahistidine-Ni 2+-NTA and N-acetylhexahistidine-Cu 2+-NTA were 69.5 M and 27.1 M, respectively. Decreased number of histidine residues in the oligohistidine fragment caused gradual decrease in the stability of the mixed metal complexes and a change in the binding stoichiometry from ~ 1:1 for N-acetylhexahistidine and N-acetylpentahistidine to ~ 0.5:1 for Nacetyltetrahistidine and ~ 0.3:1 for N-acetyltrihistidine, N-acetyldihistidine and N-acetylhistidine ligands. In all Ac(His) 1-6 COO-NTA-M 2+-Ac(His) 1-6 COO

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Studies on Complexation in Solution with a Paper Electrophoretic Technique [The System Copper(II)/Cobalt(II)−Methionine−Penicillamine]

Tewari

2010

J. Chem. Eng. Data

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Complexation reactions of methionine and penicillamine with copper(II) and cobalt(II) have been studied in the solution phase using a paper ionophoretic technique. This method is based on the movement of a spot of metal ion in an electric field with the complexants added in the background electrolyte at pH 8.5. The concentration of primary ligand methionine was kept constant, while that of the secondary ligand penicillamine was varied. A plot of log[penicillamine] versus mobility was used to obtain information on the mixed complexes and to calculate stability constants. The stability constants of the complexes copper(II)-methioninepenicillamine and cobalt(II)-methionine-penicillamine have been found to be 3.65 ( 0.03 and 3.05 ( 0.07 (logarithm stability constant values), respectively, at a temperature of 35 °C and ionic strength of 0.1 M. † Part of the "Josef M. G. Barthel Festschrift".

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Metal‐Chelating Amino Acids as Building Blocks for Synthetic Receptors Sensing Metal Ions and Histidine‐Tagged Proteins.

Cited by 4 publications

References 1 publication

Highly-Efficient Purification of Native Polyhistidine-Tagged Proteins by Multivalent NTA-Modified Magnetic Nanoparticles

Highly-Efficient Purification of Native Polyhistidine-Tagged Proteins by Multivalent NTA-Modified Magnetic Nanoparticles

Calorimetric studies of ternary complexes of Ni(II) and Cu(II) nitrilotriacetic acid and N-acetyloligohistidines

Studies on Complexation in Solution with a Paper Electrophoretic Technique [The System Copper(II)/Cobalt(II)−Methionine−Penicillamine]

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