Oriented immobilisation of anti-pneumolysin Fab through a histidine tag for electrochemical immunosensors

Vallina-García, Romina; García-Suárez, María del Mar; Fernández‐Abedul, M. Teresa; Méndez, Francisco Javier; Costa-Garcı́a, Agustı́n

doi:10.1016/j.bios.2007.04.001

Cited by 30 publications

(16 citation statements)

References 28 publications

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“…1c). Surfaces such as a glass plate deposited with Au (Nakaji-Hirabayashi et al, 2007;Vallina-García et al, 2007), a maleic-anhydride-activated polystyrene plate (Paborsky et al, 1996), or PEG-coated Si(III) (Cha et al, 2004(Cha et al, , 2005 can be used, on which a chelate group, i.e., di-or trivalent carboxylic acids such as imidoacetic acid (IDA) and nitrotriacetic acid (NTA), is attached to form a self-assembled monolayer (SAM). The chelate group strongly binds to Ni +2 or Cu +2 via three or four binding sites, leaving three or two respectively vacant sites for coordination to imidazole groups of the tagged protein molecule (Cha et al, 2004).…”

Section: Hisx6-tag Mediated Immobilizationmentioning

confidence: 99%

“…They concluded that the developed substrate provides an efficient method for the highly selective expansion of NSCs. Vallina-García et al, (2007) studied the orientation of recombinant Hisx6-tagged Fab fragments of a monoclonal antibody on Au film using an alkanethiol that terminates with a NTA group chelating Ni 2+ as a linker between the Au film and the Hisx6-tagged Fab fragment. No improvement of antigen detection was obtained in comparison with the direct adsorption.…”

Section: Hisx6-tag Mediated Immobilizationmentioning

confidence: 99%

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Recent Advances in Controlled Immobilization of Proteins onto the Surface of the Solid Substrate and Its Possible Application to Proteomics

Nakanishi¹,

Sakiyama²,

Kumada³

et al. 2008

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Proteome analysis plays a key role in the elucidation of the functions and applications for numerous proteins. For proteome analyses, various microplate-and microarray-based techniques have been developed by a number of researchers. Their intent was to immobilize proteins on the surface of a solid substrate in a site-directed manner while retaining structure and native biological function. In this review, we focus on recent advances in immobilization methodology for proteins/enzymes on a surface, including those using the affinity peptides screened by random peptide library systems. We also discuss applications of the affinity peptide-mediated immobilization method in fields related to proteome analysis, particularly our recent work concerning immunoassay and protein-protein interaction analysis.

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Section: Hisx6-tag Mediated Immobilizationmentioning

confidence: 99%

Section: Hisx6-tag Mediated Immobilizationmentioning

confidence: 99%

Recent Advances in Controlled Immobilization of Proteins onto the Surface of the Solid Substrate and Its Possible Application to Proteomics

Nakanishi¹,

Sakiyama²,

Kumada³

et al. 2008

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“…On the other hand gold can be used as an electrode for the electrochemical studies of the immobilized proteins [31], where the mediated electrical communication of an enzyme [25,[32][33][34] or antibody orientation [35] or an allosteric protein [19,28] with the gold electrode can be finely tuned through protein orientations on the SAM.…”

Section: Introductionmentioning

confidence: 99%

Direct reagentless detection of the affinity binding of recombinant His-tagged firefly luciferase with a nickel-modified gold electrode

Vagin

Trashin

Белоглазкина

et al. 2015

Mendeleev Communications

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The direct reagentless electrochemical detection of recombinant firefly luciferase binding with gold electrode modified with nickel ions has been carried out. Self-assembly of molecules of functional disulfide containing chelating moieties on the gold electrode was monitored by contact angle measurements and confirmed by electrochemical data as three times decrease of electric double layer capacitance. Succeeding nickel ions chelating followed by selective binding of target protein were registered by reagentless electrochemical measurements as consistent decreases of double layer capacitance. The quantification of bound protein has been achieved by means of luminescent assay of residual enzymatic activity in solution for electrode recovery. The electrode surface coverage by protein globules has been confirmed by AFM.

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“…The Pichia system allowing the production of heterologous proteins is among the most popular [1–3]. Most often a polyhistidine-tag consists of six histidine residues at the C- or N-terminus of the proteins (His 6 -tag).…”

Section: Introductionmentioning

confidence: 99%

Immunosensor Incorporating Anti-His (C-term) IgG F(ab’) Fragments Attached to Gold Nanorods for Detection of His-Tagged Proteins in Culture Medium

Wąsowicz

Milner

Radecka

et al. 2010

Sensors

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Immunosensors based on gold electrodes (electrochemical) or gold discs (optical) modified with 1,6-hexanedithiol, gold nanorods and Anti-His (C-term) monoclonal antibody F(ab’) fragment are described. The antigen detected by the sensing platform is a recombinant histidine-tagged silk proteinase inhibitor (rSPI2-His6). Electrochemical impedance spectroscopy (EIS) and surface plasmon resonance (SPR) techniques were used as methods for detection of the antigen. This approach allows to detect the antigen protein in concentration of 10 pg per mL (0.13 pM) of culture medium. The immunosensor shows good reproducibility due to covalent immobilization of F(ab’) fragments to gold nanorods layer.

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Oriented immobilisation of anti-pneumolysin Fab through a histidine tag for electrochemical immunosensors

Cited by 30 publications

References 28 publications

Recent Advances in Controlled Immobilization of Proteins onto the Surface of the Solid Substrate and Its Possible Application to Proteomics

Recent Advances in Controlled Immobilization of Proteins onto the Surface of the Solid Substrate and Its Possible Application to Proteomics

Direct reagentless detection of the affinity binding of recombinant His-tagged firefly luciferase with a nickel-modified gold electrode

Immunosensor Incorporating Anti-His (C-term) IgG F(ab’) Fragments Attached to Gold Nanorods for Detection of His-Tagged Proteins in Culture Medium

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