Nonperturbative Chemical Modification of Graphene for Protein Micropatterning

Kodali, Vamsi; Scrimgeour, Jan; Kim, Suenne; Hankinson, John; Carroll, Keith M.; Heer, Walt A. de; Berger, Claire; Curtis, Jennifer E.

doi:10.1021/la1033178

Cited by 85 publications

(59 citation statements)

References 31 publications

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“…In contrast, G and D bands appeared at 1590 and 1349 cm À1 , respectively for SAC-RGO. 51 It is worth noting that the basal arrangement of the graphitic domains was signicantly improved, which was evaluated by its I D /I G ratios. 48 The changes in I D /I G (I D ¼ intensity of D band, I G intensity of G band in Raman spectra) ratios can provide information about the variable ratios of C sp3 /C sp2 of a graphite moiety.…”

Section: Resultsmentioning

confidence: 99%

Non-covalent functionalization of reduced graphene oxide using sulfanilic acid azocromotrop and its application as a supercapacitor electrode material

et al. 2015

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Sulfanilic acid azocromotrop (SAC) modified reduced graphene oxide (SAC-RGO) was prepared by simple non-covalent functionalization of graphene oxide (GO) followed by post reduction using hydrazine monohydrate. Spectral analysis (Fourier transform infrared, Raman and X-ray photoelectron spectroscopy) revealed that successful modification had occurred of GO with SAC through p-p interaction. The electrical conductivity of SAC-RGO was found to be $551 S m À1 . The capacitive performance of SAC-RGO was recorded using a three electrode set up with 1 (M) aqueous H 2 SO 4 as the electrolyte. The -SO 3 H functionalities of SAC contributed pseudocapacitance as evidenced from the redox peaks (at $0.43 and 0.27 V) present in the cyclic voltammetric (CV) curves measured for SAC-RGO. The contribution of electrical double layer capacitance was evidenced from the near rectangular shaped CV curves and resulted in a high specific capacitance of 366 F g À1 at a current density of 1.2 A g À1 for SAC-RGO electrode. An asymmetric device (SAC-RGO//RGO) was designed with SAC-RGO as the positive electrode and RGO as the negative electrode. The device showed an energy density of $25.8 W h kg À1 at a power density of $980 W kg À1 . The asymmetric device showed retention in specific capacitance of $72% after 5000 charge-discharge cycles. The Nyquist data of the device was fitted with Z-view and different components (solution resistance, charge-transfer resistance and Warburg elements) were calculated from the fitted curves.

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Section: Resultsmentioning

confidence: 99%

Non-covalent functionalization of reduced graphene oxide using sulfanilic acid azocromotrop and its application as a supercapacitor electrode material

et al. 2015

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“…We use 1-Pyrenebutyric acid N-hydroxysuccinimide ester (PYR-NHS, Sigma-Aldrich) as a bifunctional linker 30,31 to functionalize GFETs with wsMOR (See Methods in Supporting information). Atomic Force Microscopy shows that the density of wsMOR bound to the GFET surface is ~115 μm −2 (Fig.…”

Section: Methodsmentioning

confidence: 99%

Quantifying the effect of ionic screening with protein-decorated graphene transistors

Ping

Jin

Saven

et al. 2017

Biosensors and Bioelectronics

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Liquid-based applications of biomolecule-decorated field-effect transistors (FETs) range from biosensors to in vivo implants. A critical scientific challenge is to develop a quantitative understanding of the gating effect of charged biomolecules in ionic solution and how this influences the readout of the FETs. To address this issue, we fabricated protein-decorated graphene FETs and measured their electrical properties, specifically the shift in Dirac voltage, in solutions of varying ionic strength. We found excellent quantitative agreement with a model that accounts for both the graphene polarization charge and ionic screening of ions adsorbed on the graphene as well as charged amino acids associated with the immobilized protein. The technique and analysis presented here directly couple the charging status of bound biomolecules to readout of liquid-phase FETs fabricated with graphene or other two-dimensional materials.

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“…The procedure involves actually both noncovalent and covalent binding interactions. This strategy should be useful for massive preparations of parallel biosensors, gene chips, electronic devices, and other multifunctional surface nanoarchitectures [126] .…”

Section: Covalently Binding Enzyme/protein On Gomentioning

confidence: 99%

Interactions of graphene and graphene oxide with proteins and peptides

Zhang

Guo³

et al. 2013

Nanotechnology Reviews

208

107

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This review selectively describes the recent progress in the interactions of proteins (enzymes) and shortchain peptides with graphene and graphene oxide (GO). Particularly, the advances of the immobilization mechanisms of enzymes on graphene and GO, the catalytic properties of the immobilized enzymes, and their applications are summarized in detail. The interfacings of the peptides with graphene and GO, the as assembled conjugates, and their potential applications are discussed briefly. The possible ongoing development for the assembly of conjugates of graphene and GO with proteins and peptides in a controlled manner is speculated upon.

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Nonperturbative Chemical Modification of Graphene for Protein Micropatterning

Cited by 85 publications

References 31 publications

Non-covalent functionalization of reduced graphene oxide using sulfanilic acid azocromotrop and its application as a supercapacitor electrode material

Non-covalent functionalization of reduced graphene oxide using sulfanilic acid azocromotrop and its application as a supercapacitor electrode material

Quantifying the effect of ionic screening with protein-decorated graphene transistors

Interactions of graphene and graphene oxide with proteins and peptides

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