Electrocatalytically active multi-protein assemblies using nanoscaled building blocks

Feifel, Sven C.; Kapp, Andreas; Ludwig, Roland; Gorton, Lo; Lisdat, Fred

doi:10.1039/c2ra22819j

Cited by 10 publications

(8 citation statements)

References 51 publications

(50 reference statements)

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“…[2] A key issue in the development of any biosensor is its sensitivity, which in the case of amperometric biosensors is controlled by several factors, such as substrate diffusion, redox mediator features, and the electrical communication between the recognition element and the other device components. [7] In the past several years, carbon nanotubes [8] (CNTs) and gold nanoparticles [9] (AuNPs) have shown excellent electrocatalytic properties, which were immediately applied to the development of biosensors. To overcome this limitation, a wide variety of surface-functionalization strategies, such as self-assembled monolayers, [3] polymers, [4] proteic coatings, [5] and hydrogels, [6] have been explored to preserve the native structure and function of the incorporated enzyme.…”

Section: Introductionmentioning

confidence: 99%

“…To overcome this limitation, a wide variety of surface-functionalization strategies, such as self-assembled monolayers, [3] polymers, [4] proteic coatings, [5] and hydrogels, [6] have been explored to preserve the native structure and function of the incorporated enzyme. [7] In the past several years, carbon nanotubes [8] (CNTs) and gold nanoparticles [9] (AuNPs) have shown excellent electrocatalytic properties, which were immediately applied to the development of biosensors. [10] Particularly, the inclusion of AuNPs was intended to allow direct electron transfer, in which the electrons can directly tunnel from the catalytic center of the enzyme to the surface of the current collector, [11] even though this strategy presents some limitations.…”

Section: Introductionmentioning

confidence: 99%

“…The most studied example is the glucose biosensor, where the efficient electrical communication between the biological recognition element (GOx) and the transducer (the mediator/working electrode interface) is often challenged by the enzyme’s insulating shell of amino acids. To overcome this limitation, a wide variety of surface‐functionalization strategies, such as self‐assembled monolayers,3 polymers,4 proteic coatings,5 and hydrogels,6 have been explored to preserve the native structure and function of the incorporated enzyme 7…”

Section: Introductionmentioning

confidence: 99%

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Effect of Gold Nanoparticles on the Structure and Electron‐Transfer Characteristics of Glucose Oxidase Redox Polyelectrolyte‐Surfactant Complexes

Cortez

Marmisollé

Pallarola

et al. 2014

Chemistry A European J

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Efficient electrical communication between redox proteins and electrodes is a critical issue in the operation and development of amperometric biosensors. The present study explores the advantages of a nanostructured redox-active polyelectrolyte-surfactant complex containing [Os(bpy)2Clpy](2+) (bpy=2,2'-bipyridine, py= pyridine) as the redox centers and gold nanoparticles (AuNPs) as nanodomains for boosting the electron-transfer propagation throughout the assembled film in the presence of glucose oxidase (GOx). Film structure was characterized by grazing-incidence small-angle X-ray scattering (GISAXS) and atomic force microscopy (AFM), GOx incorporation was followed by surface plasmon resonance (SPR) and quartz-crystal microbalance with dissipation (QCM-D), whereas Raman spectroelectrochemistry and electrochemical studies confirmed the ability of the entrapped gold nanoparticles to enhance the electron-transfer processes between the enzyme and the electrode surface. Our results show that nanocomposite films exhibit five-fold increase in current response to glucose compared with analogous supramolecular AuNP-free films. The introduction of colloidal gold promotes drastic mesostructural changes in the film, which in turn leads to a rigid, amorphous interfacial architecture where nanoparticles, redox centers, and GOx remain in close proximity, thus improving the electron-transfer process.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Effect of Gold Nanoparticles on the Structure and Electron‐Transfer Characteristics of Glucose Oxidase Redox Polyelectrolyte‐Surfactant Complexes

Cortez

Marmisollé

Pallarola

et al. 2014

Chemistry A European J

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“…36 Similarly, the enzyme cellobiose dehydrogenase (CDH) could be incorporated into a cyt c-DNA architecture to afford the system a sensitivity towards lactose, the enzyme's substrate. 40 These developments illustrate the application potential for cyt c-DNA interactions but they are not limited to bio-electrochemistry, since actual developments in creating 3D-structures made from nucleic acids can also pave the way for a defined positioning of proteins in bio-hybrid systems. [14][15][16] Although the electrostatic nature of the cyt c-DNA interaction was already studied, little is known about the structural details and the pH dependence.…”

Section: Introductionmentioning

confidence: 99%

Study of Cytochrome c-DNA Interaction – Evaluation of Binding Sites on the Redox Protein

et al. 2014

Self Cite

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Artificial assemblies consisting of the cationic cytochrome c (cyt c) and double-stranded DNA are interesting for the field of biohybrid systems because of the high electro-activity of the incorporated redox protein. However, little is known about the interactions between these two biomolecules. Here, the complex of reduced cyt c and a 41 base pair oligonucleotide was characterized in solution as a function of pH and ionic strength. Persistent cyt c-DNA agglomerates were observed by UV-vis and DLS (dynamic light scattering) at pH 5.0 and low ionic strength. The strength of the interaction was attenuated by raising the pH or the ionic strength. At pH 7.0 agglomerates were not formed, allowing interaction analysis by NMR spectroscopy. Using TROSY (transverse relaxation-optimized spectroscopy)-HSQC (heteronuclear single quantum coherence) experiments it was possible to identify the DNA binding site on the cyt c surface. Numerous residues surrounding the exposed heme edge of cyt c were involved in transient binding to DNA under these conditions. This result was supported by SEC (size exclusion chromatography) experiments at pH 7.0 showing that the interaction is sufficient for co-elution of cyt c and DNA.

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“…Most research works were carried out in the presence of cytochrome c (Cyt c). [4][5][6] The direct electrochemical research on Cyt c is also the foundation to develop new electrochemical sensors. The electrochemical processes of Cyt c have been widely studied in order to understand electron transfer mechanisms in biological systems.…”

Section: Introductionmentioning

confidence: 99%

The electrochemical studies of cytochrome c incorporated in 3D porous calcium alginate films on glassy carbon electrodes

Jian¹,

Liu²,

Sun³

et al. 2014

RSC Adv.

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In this work, the cytochrome c (Cyt c) was incorporated in three-dimension (3D) porous calcium alginate (CA) films prepared by using sodium alginate, calcium chloride and polyethylene glycol, and formed the electroactive porous Cyt c-CA composite films. The stable composite films were characterized by means of scanning electron microscopy (SEM), UV-vis absorption, cyclic voltammetry (CV) and squarewave voltammetry (SWV) techniques. UV-vis experiments demonstrated that Cyt c assembled in the 3D porous CA films retains its near native conformation at medium pH. The Cyt c-CA films modified on glassy carbon electrodes showed a pair of well-defined and nearly reversible cyclic voltammetry peaks at about À0.352 V vs. SCE in protein-free buffer, which originated from heme Fe III/II redox couples within Cyt c. The electrochemical parameters such as apparent heterogeneous electron transfer rate constant (k s ) and formal potential (E o 0 ) were estimated by fitting the data of SWV with nonlinear regression analysis. The Cyt c-CA films showed the electrocatalytic activity toward dioxygen, hydrogen peroxide, nitrite and trichloroacetic acid with significant decreases in the electrode potential required. Experimental data demonstrated that the porous film can provide a favorable microenvironment for the protein to directly transfer electrons with the underlying electrode and possess good stability and reproducibility, showing the possible future application of the films for biosensors and biocatalysis.

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Electrocatalytically active multi-protein assemblies using nanoscaled building blocks

Cited by 10 publications

References 51 publications

Effect of Gold Nanoparticles on the Structure and Electron‐Transfer Characteristics of Glucose Oxidase Redox Polyelectrolyte‐Surfactant Complexes

Effect of Gold Nanoparticles on the Structure and Electron‐Transfer Characteristics of Glucose Oxidase Redox Polyelectrolyte‐Surfactant Complexes

Study of Cytochrome c-DNA Interaction – Evaluation of Binding Sites on the Redox Protein

The electrochemical studies of cytochrome c incorporated in 3D porous calcium alginate films on glassy carbon electrodes

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