A switchable peroxidase mimic derived from the reversible co-assembly of cytochrome c and carbon dots

Essner, Jeremy B.; McCay, Richard N.; Smith, Chip J.; Cobb, Stephen M.; Laber, Charles H.; Baker, Gary A.

doi:10.1039/c6tb00052e

Cited by 17 publications

(22 citation statements)

References 37 publications

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“…Channel blocking inhibitors were also tested due to CND’s known ability for having a slight negative charge [ 33 , 34 ]. HMEC-1s were this time treated for 30 min with known channel blocking inhibitors at concentrations from previously completed research ( Table 1 ).…”

Section: Resultsmentioning

confidence: 99%

Anti-Inflammatory Effect and Cellular Uptake Mechanism of Carbon Nanodots in in Human Microvascular Endothelial Cells

et al. 2021

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Cardiovascular disease (CVD) has become an increasingly important topic in the field of medical research due to the steadily increasing rates of mortality caused by this disease. With recent advancements in nanotechnology, a push for new, novel treatments for CVD utilizing these new materials has begun. Carbon Nanodots (CNDs), are a new form of nanoparticles that have been coveted due to the green synthesis method, biocompatibility, fluorescent capabilities and potential anti-antioxidant properties. With much research pouring into CNDs being used as bioimaging and drug delivery tools, few studies have been completed on their anti-inflammatory potential, especially in the cardiovascular system. CVD begins initially by endothelial cell inflammation. The cause of this inflammation can come from many sources; one being tumor necrosis factor (TNF-α), which can not only trigger inflammation but prolong its existence by causing a storm of pro-inflammatory cytokines. This study investigated the ability of CNDs to attenuate TNF-α induced inflammation in human microvascular endothelial cells (HMEC-1). Results show that CNDs at non-cytotoxic concentrations reduce the expression of pro-inflammatory genes, mainly Interleukin-8 (IL-8), and interleukin 1 beta (IL-1β). The uptake of CNDs by HMEC-1s was examined. Results from the studies involving channel blockers and endocytosis disruptors suggest that uptake takes place by endocytosis. These findings provide insights on the interaction CNDs and endothelial cells undergoing TNF-α induced cellular inflammation.

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Section: Resultsmentioning

confidence: 99%

Anti-Inflammatory Effect and Cellular Uptake Mechanism of Carbon Nanodots in in Human Microvascular Endothelial Cells

et al. 2021

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“…7b), which further induces the conformational changes of the β-sheet and the changes of its microenvironment indicated by the shift of band frequency. Such changes could also affect the microenvironment of heme since these residues are connected with heme propionate, which might facilitate the coordinate of H2O2, resulting in the enhanced electrocatalytic activity of adsorbed cyt c towards H2O2 reduction [42][43][44]. Moreover, such interaction could slightly change the adsorption orientation of adsorbed cyt c with heme more perpendicular to the surface as shown in Fig.…”

Section: Seiras and Potential-induced Seira Difference Spectroscopy Smentioning

confidence: 94%

“…For a partially unfolded cyt c [39,47], its oxidized form always opens the heme crevice due to the change of ligand so as to have a large solvent accessibility of the heme, while its reduced form possesses a relatively compact conformation, which determines the negative shift of its formal potential relative to native cyt c. Since the structure and related heme microenvironment of cyt c treated with SiO2 NPs were changed in the oxidized form while were kept in the reduced form relative to those of native cyt c as shown in Fig. 6d, a similar hydration degree could be proposed for both cyt c (Fe 2+ ) and a more hydrophilic microenvironment for cyt c (Fe 3+ ) treated by SiO2 NPs, and thus a higher dielectric constant environment, which could result in the slight negative shift of the formal potential relative to that of native cyt c. In addition, the adsorption of negatively charged SiO2 NPs could compensate the surface charge of cyt c/MUA/Au, which could induce the change of surface potential, resulting in slight negative shift in the formal potential of adsorbed cyt c [43].…”

Section: Seiras and Potential-induced Seira Difference Spectroscopy Smentioning

confidence: 96%

Surface-enhanced infrared absorption spectroscopy and electrochemistry reveal the impact of nanoparticles on the function of protein immobilized on mimic biointerface

Zhang

Zeng

Liu

et al. 2016

Electrochimica Acta

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Surface-enhanced infrared absorption spectroscopy and electrochemistry reveal the impact of nanoparticles on the function of protein immobilized on mimic biointerface, Electrochimica Acta http://dx. AbstractStudy of the interactions between engineered nanoparticles and biomolecules plays an important role in understanding nano-bio effect. However, most of studies focus on the interaction of protein with nanoparticle in bulk phase, the impact of nanoparticle on the function of protein immobilized on the biological interface has been ignored for a long time. In this paper, we study the effect of SiO2 NPs on electron transfer function of cytochrome c (cyt c) adsorbed onto the 11-mercaptoundecanoic acid (MUA) self-assembled monolayer (SAM) by surface-enhanced infrared absorption spectroscopy (SEIRAS) combined with electrochemistry. Our results disclose that instead of inhibiting the electron transfer, exposure of SiO2 NPs enhances the redox reversibility, electron transfer rate, and catalytic performance of adsorbed cyt c, but induces a slight negative shift in the formal potential of the adsorbed cyt c. Interaction of SiO2 NPs slightly induces the structural changes of the β-sheet in the oxidized form and the change of microenvironment surrounding them, which could further change the microenvironment and the orientation of heme, facilitating the hydration of cyt c at the oxidized state. It could be the enhanced hydration of cyt c (Fe 3+ ) and a smaller change in the total hydration from reduced to oxidized state that results in the slight negative shift in the formal potential and promotes the electron transfer capability. Besides, cyt c's slight conformational change and the disturbance to the microenvironment of heme resulting from the adsorption of SiO2 NPs could also be one of the reason that leads to the enhanced catalytic capability towards the reduction of H2O2.

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“…Very recently, Baker and co-workers [54] have reported a straightforward tactic to boost the low POD-like activity of cytochrome c (cyt c ), an electron transfer protein in the respiratory chain, following its electrostatic assembly onto the C-dots surface. Specifically, citric acid (CA) as a carbon source was thermally carbonized alone as well as in the presence of various dopants/passivating agents such as urea (U), thiourea (T) and mercaptosuccinic acid (M), to generate four different CA, CA-U, CA-T, and CA-M-derived C-dots.…”

Section: Gqds/c-dots Conjugates And/or Nanocomposites As Pod Nanozmentioning

confidence: 99%

“…( A ) Neat carbon nanodots (C-dots) did not display any catalytic activity, as evidenced by the lack of green color in ( Ai ); while native cytochrome c (cyt c ) was found to exhibit weak peroxidase activity ( Aii ); When C-dots were combined with cyt c , the peroxidase activity was dramatically enhanced, indicated by the rapid formation of the oxidized form of ABTS (i.e., appearance of intense green color), as shown in ( Aiii ); ( B ) Different orientations of the electrostatic calculations performed on cyt c show that a majority of the protein surface is positively charged (blue areas), with the bulk of the positive charge residing in the vicinity of the heme group. Reproduced from [54]. …”

Section: Figures Schemes and Tablesmentioning

confidence: 99%

Carbon Nanodots as Peroxidase Nanozymes for Biosensing

Garg

Bisht²

2016

Molecules

130

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'Nanozymes', a term coined by Scrimin, Pasquato, and co-workers to describe nanomaterials with enzyme-like characteristics, represent an exciting and emerging research area in the field of artificial enzymes. Indubitably, the last decade has witnessed substantial advancements in the design of a variety of functional nanoscale materials, including metal oxides and carbon-based nanomaterials, which mimic the structures and functions of naturally occurring enzymes. Among these, carbon nanodots (C-dots) or carbon quantum dots (CQDs) offer huge potential due to their unique properties as compared to natural enzymes and/or classical artificial enzymes. In this mini review, we discuss the peroxidase-like catalytic activities of C-dots and their applications in biosensing. The scope intends to cover not only the C-dots but also graphene quantum dots (GQDs), doped C-dots/GQDs, carbon nitride dots, and C-dots/GQDs nanocomposites. Nevertheless, this mini review is designed to be illustrative, not comprehensive.

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A switchable peroxidase mimic derived from the reversible co-assembly of cytochrome c and carbon dots

Abstract: We describe a straightforward tactic to boost the inherently low peroxidase-like activity of the heme-protein equine cytochrome c following its electrostatic assembly onto the carbon nanodot surface.

Cited by 17 publications

References 37 publications

Anti-Inflammatory Effect and Cellular Uptake Mechanism of Carbon Nanodots in in Human Microvascular Endothelial Cells

Anti-Inflammatory Effect and Cellular Uptake Mechanism of Carbon Nanodots in in Human Microvascular Endothelial Cells

Surface-enhanced infrared absorption spectroscopy and electrochemistry reveal the impact of nanoparticles on the function of protein immobilized on mimic biointerface

Carbon Nanodots as Peroxidase Nanozymes for Biosensing

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