Immobilization of histidine-tagged proteins on electrodes

Ley, Claudia; Holtmann, Dirk; Mangold, Klaus‐Michael; Schrader, Jens

doi:10.1016/j.colsurfb.2011.07.044

Cited by 79 publications

(56 citation statements)

References 64 publications

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“…The study of the behavior of this amino acid is important due to the possibility of using a L-His tag at the end of designed proteins to facilitate their isolation since its side chain adsorbs onto metallic electrodes (Ley et al 2011, Ogura et al 1999. The electrochemical behavior of this molecule, according to the literature (Chen et al 2008), is still not clear; it seems to be more sensitive to the electrode nature than other amino acids previously discussed.…”

Section: Electrochemically Active Amino Acidsmentioning

confidence: 91%

The long and successful journey of electrochemically active amino acids. From fundamental adsorption studies to potential surface engineering tools.

Dourado

Pastrián

Torresi

2018

An. Acad. Bras. Ciênc.

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Proteins have been the subject of electrochemical studies. It is possible to apply electrochemical techniques to obtain information about their structure due to the presence of five electroactive amino acids that can be oriented to the outside of the peptidic chain. These amino acids are L-and L-Cysteine (L-Cys); their electrochemical behavior being subject of extensive research, but it is still controversial. No spectroscopic investigations have been reported on L-Trp, and due to the short life time of the intermediates, ex situ techniques cannot be employed, leading to a never-ending discussion about possible intermediates. In the L-Tyr and L-His cases, spectroelectrochemical studies were performed and different intermediates were observed, suggesting that some intermediates may be observed under specific conditions, as proposed for L-Cys. This amino acid is the most interesting among the electroactive ones because of the presence of a thiol moiety at its side chain, leading to a wide range of oxidation states. It can adsorb onto surfaces of different crystallographic orientation in stereoselective conformation, modifying the surface for different applications.as a surface engineering tool since it plays the role of as an anchor for the growing of nanocrystals inside proteic templates.

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Section: Electrochemically Active Amino Acidsmentioning

confidence: 91%

The long and successful journey of electrochemically active amino acids. From fundamental adsorption studies to potential surface engineering tools.

Dourado

Pastrián

Torresi

2018

An. Acad. Bras. Ciênc.

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“…Samples with immobilized ligand-free GBP are also prepared for comparison. In this design, glucosebinding protein is attached to surface by means of a histidine tag, which binds well to Ni but not to noble metals 6 . Since the substrates comprise arrays of Ag nano-dots, nano-hexagons, and unstructured Ag pads on Ni-coated FS (Figures 6B, 6D, and 6F, respectively), one can expect most of immobilized protein molecules to be located in gaps between Ag nanostructures where Ni coating is available.…”

Section: Representative Resultsmentioning

confidence: 99%

“…This involves multidisciplinary studies across a number of research fields, such as the fabrication of pertinent solid-state components (micro-or nano-electrodes, nano-engineered coatings, nanowires, or nanoparticles) 2,3,4 ; immobilization of biomolecules on the surfaces to create desired bioconjugates 5,6,7 ; and monitoring nano-biological interfaces 1 . In most cases, the selection of optimal fabrication, bio-functionalization, and characterization methods is strongly inter-related.…”

Section: Introductionmentioning

confidence: 99%

Surface Enhanced Raman Spectroscopy Detection of Biomolecules Using EBL Fabricated Nanostructured Substrates

Peters

Gutierrez-Rivera

Dew

et al. 2015

JoVE

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Fabrication and characterization of conjugate nano-biological systems interfacing metallic nanostructures on solid supports with immobilized biomolecules is reported. The entire sequence of relevant experimental steps is described, involving the fabrication of nanostructured substrates using electron beam lithography, immobilization of biomolecules on the substrates, and their characterization utilizing surface-enhanced Raman spectroscopy (SERS). Three different designs of nano-biological systems are employed, including protein A, glucose binding protein, and a dopamine binding DNA aptamer. In the latter two cases, the binding of respective ligands, D-glucose and dopamine, is also included. The three kinds of biomolecules are immobilized on nanostructured substrates by different methods, and the results of SERS imaging are reported. The capabilities of SERS to detect vibrational modes from surface-immobilized proteins, as well as to capture the protein-ligand and aptamer-ligand binding are demonstrated. The results also illustrate the influence of the surface nanostructure geometry, biomolecules immobilization strategy, Raman activity of the molecules and presence or absence of the ligand binding on the SERS spectra acquired.

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“…The His-tag typically consists of five or six consecutive His residues added to the C-or N-terminus of the protein [20]. The most popular systems for oriented immobilization of His-tagged proteins are complexes of nitrilotriacetic acid (NTA) or iminodiacetic acid (IDA) with transition metal ions (Ni 2+ , Cu 2+ ) [20][21][22][23][24][25][26][27][28]. Nitrilotriacetic acid forms a tetradentatechelate with Ni 2+ and Cu 2+ , which is able to bind His-tagged proteins via coordinated bonds [29].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of His-tagged kinase JAK2 onto the surface of a plasmon resonance gold disc modified with different copper (II) complexes

Kurzątkowska¹,

Mielecki²,

Grzelak³

et al. 2014

Talanta

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New surface plasmon resonance (SPR) sensing platform swhich consists of copper (II) complexes of a pentetic acid thiol ligand (DPTA-Cu(II)) and of a thiol derivative of dipyrromethene (DPM-Cu(II) created on the surface of gold SPR disc were applied to oriented immobilization of His-tagged Janus kinase 2 (GST-His 6 -JAK2). This method is based on the covalent bond formation between histidine from a His-tag chain of a protein and Cu(II) centres from the complexes. The kinetic and thermodynamic parameters of the oriented immobilization of GST-His 6 -JAK2 protein to DPTA-Cu(II) and DPM-Cu(II) complexes attached to the Au surface of a SPR disc were discussed.

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Immobilization of histidine-tagged proteins on electrodes

Cited by 79 publications

References 64 publications

The long and successful journey of electrochemically active amino acids. From fundamental adsorption studies to potential surface engineering tools.

The long and successful journey of electrochemically active amino acids. From fundamental adsorption studies to potential surface engineering tools.

Surface Enhanced Raman Spectroscopy Detection of Biomolecules Using EBL Fabricated Nanostructured Substrates

Immobilization of His-tagged kinase JAK2 onto the surface of a plasmon resonance gold disc modified with different copper (II) complexes

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