Electrochemical sensing of cytochrome c using Graphene Oxide nanoparticles as platform

Batra, Bhawna; Sangwan, Samiksha; Ahlawat, Jyoti; Sharma, Minakshi

doi:10.1016/j.ijbiomac.2020.09.203

Cited by 10 publications

(4 citation statements)

References 31 publications

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“…In particular, four of the most important peaks responsible for the structural features of Cyt c are 1391, 1538, 1644, and 3290 cm −1 (Figure 4a,b), which correspond to CH 3 symmetric stretching, amide I band (80% C�O stretch), amide II band (60% N−H and 40% C−N), and amide A band (mainly N−H stretching), respectively. 56,57 The FTIR spectra of the native Cyt c match very well with the literature. 51 As depicted in Figure 4, there is no significant wavenumber shift in amide I and II bands upon addition of MNPs, indicating Cyt c's secondary structure is undestroyed in the presence of MNPs.…”

Section: Fourier Transform Infrared (Ftir) and Raman Spectroscopy Stu...supporting

confidence: 81%

Impact of Choline Hydroxide-Supported Magnetic Nanoparticles on Peroxidase Activity and Conformational Stability of Cytochrome c

Chahar,

Jha,

Arumugam

et al. 2024

ACS Appl. Bio Mater.

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Nanotechnology has advanced significantly; however, little is known about the potential implications on human health-related issues, particularly blood carrying enzymes. Ionic liquids are also well-recognized for maintaining the structure and activity of enzymes. In this regard, we delineate a facile synthetic approach of preparation of Fe 3 O 4 nanoparticles (NPs) as well as choline hydroxide [CH][OH] ionic liquid (IL)-supported Fe 3 O 4 NPs (Fe 3 O 4 −CHOH). This approach of combining magnetic nanoparticles (MNPs) with IL results in distinctive properties, which may offer enormous utility in the field of biomedical research due to the effortless separation of MNPs by an external magnetic field. Detailed characterization of MNPs including Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), Raman spectroscopy, transmission electron microscopy (TEM), and scanning electron microscopy (SEM) was carried out. The biomolecular interactions of Fe 3 O 4 and Fe 3 O 4 −CHOH NPs with cytochrome c (Cyt c) were studied in detail using various spectroscopic and microscopic techniques. From spectroscopic studies, it can be concluded that the secondary structure of Cyt c is more stable in the presence of Fe 3 O 4 −CHOH NPs than Fe 3 O 4 NPs. The binding constant of Cyt c in the presence of MNPs was also calculated using the Benesi−Hildebrand equation. Furthermore, dynamic light scattering (DLS), ζ-potential, and microscopic studies were performed to study the interaction of Cyt c with MNPs. These studies provided evidence favoring the formation of bionanoconjugates of Cyt c with MNPs. Moreover, the enzymatic activity of Cyt c increases in the presence of both MNPs. The peroxidase activity of Cyt c in MNPs explicitly elucidates that the enzyme is preserved for a long time in the presence of Fe 3 O 4 −CHOH NPs. Later on, TEM and field emission scanning electron microscopy (FESEM) were also performed to gather more information regarding the morphology of Cyt c in the presence of MNPs.

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Section: Fourier Transform Infrared (Ftir) and Raman Spectroscopy Stu...supporting

confidence: 81%

Impact of Choline Hydroxide-Supported Magnetic Nanoparticles on Peroxidase Activity and Conformational Stability of Cytochrome c

Chahar,

Jha,

Arumugam

et al. 2024

ACS Appl. Bio Mater.

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“…These biosensors could also be tested for quantification of cyt c in human serum. Unlike in cancer, cyt c is elevated in the serum of myocardial infarction patients [ 106 ], for which some cyt c biosensors have also been developed [ 21 , 22 ]. High levels of cyt c in the serum has also been detected in HIV patients receiving antiretroviral therapy, indicating cyt c as a marker of antiretroviral toxicity in HIV patients [ 107 ].…”

Section: Discussionmentioning

confidence: 99%

“…In some of these systems, cyt c is recognized through its electrical properties. Some biosensors are based on cyt c oxidase associated to electrodes, in which electron transfer from cyt c to cyt c oxidase generates or affects electrical currents [ 21 , 22 ] ( Figure 2 A). In another electrochemical biosensor, cyt c fitting into specific recognition nanocavities lowers the electrical current established between an electrolyte solution and a gold electrode [ 23 ].…”

Section: Biosensors For Quantification Of Serum Cyt Cmentioning

confidence: 99%

Cytochrome c in cancer therapy and prognosis

Pessoa

2022

Bioscience Reports

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Cytochrome c (cyt c) is an electron transporter of the mitochondrial respiratory chain. Upon permeabilization of the mitochondrial outer membrane, cyt c is released into the cytoplasm, where it triggers the intrinsic pathway of apoptosis. Cytoplasmic cyt c can further reach the bloodstream. Apoptosis inhibition is one of the hallmarks of cancer and its induction in tumors is a widely used therapeutic approach. Apoptosis inhibition and induction correlate with decreased and increased serum levels of cyt c, respectively. The quantification of cyt c in the serum is useful in the monitoring of patient response to chemotherapy, with potential prognosis value. Several highly sensitive biosensors have been developed for the quantification of cyt c levels in human serum. Moreover, the delivery of exogenous cyt c to the cytoplasm of cancer cells is an effective approach for inducing their apoptosis. Similarly, several protein-based and nanoparticle-based systems have been developed for the therapeutic delivery of cyt c to cancer cells. As such, cyt c is a human protein with promising value in cancer prognosis and therapy. In addition, its thermal stability can be extended through PEGylation and ionic liquid storage. These processes could contribute to enhancing its therapeutic exploitation in clinical facilities with limited refrigeration conditions. Here, I discuss these research lines and how their timely conjunction can advance cancer therapy and prognosis.

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“…[ 4 ] The regular and healthy level of Cyt c in human serum is reported to be approximately 25 ng/mL (< 2 nM) [ 5 ] and in circulating blood, it is approximately 39.8 ng/mL. [ 6 ] The concentration of Cyt c is elevated in the sera of majority of the cancer patients as a result of increased cell death. Serum Cyt c has been taken as a potential and effective biomarker for diagnosing relevant diseases.…”

Section: Introductionmentioning

confidence: 99%

Luminescent gold nanoclusters as a signal reporter for cytochrome c assay with a double signal amplification strategy

Dou

2022

J Chinese Chemical Soc

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Quantitative determination of serum cytochrome c (Cyt c) is of importance in the regular medical assessment of cancer diseases. This work reported a new fluorescence method for the determination of Cyt c with glutathione‐protected gold nanoclusters (GSH‐AuNCs) as a signal reporter. Cyt c was observed to quench the fluorescence of GSH‐AuNCs due to its electron‐rich structure. This inhibitory effect was further strengthened by its peroxidase mimetic catalytic activity on hydrogen peroxide (H2O2)‐mediated oxidation of GSH‐AuNCs. The inhibitory efficiency was linearly related to Cyt c concentrations ranging from 10.0 to 700.0 nM with a limit of detection of 2.7 nM (3sb/S). The relative standard deviation was 3.6% for Cyt c at a 40.0 nM concentration level (n = 11). The practical application of the method was evaluated by the determination of Cyt c in spiked human serum samples. The recoveries were within the range from 92.6 to 104.8%, suggesting its potential application in biomedical and clinical diagnosis.

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Electrochemical sensing of cytochrome c using Graphene Oxide nanoparticles as platform

Cited by 10 publications

References 31 publications

Impact of Choline Hydroxide-Supported Magnetic Nanoparticles on Peroxidase Activity and Conformational Stability of Cytochrome c

Impact of Choline Hydroxide-Supported Magnetic Nanoparticles on Peroxidase Activity and Conformational Stability of Cytochrome c

Cytochrome c in cancer therapy and prognosis

Luminescent gold nanoclusters as a signal reporter for cytochrome c assay with a double signal amplification strategy

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