Electrochemical behavior of sarco/endoplasmic reticulum Ca-ATPase in response to carbonylation processes

Novak, David P.; Viskupičová, Jana; Zatloukalová, Martina; Heger, Vladimír; Michalikova, Silvia; Májeková, Magdaléna; Vacek, Jan

doi:10.1016/j.jelechem.2018.01.036

Cited by 6 publications

(2 citation statements)

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“…The high sensitivity of the CPS peak H to structural changes in proteins can be utilized not only for monitoring protein denaturation [ 41 – 43 ], oligomerization and aggregation [ 44 , 45 ], posttranslational modifications [ 46 – 48 ], oxidative damage [ 49 , 50 ], and single- aa replacements [ 51 , 52 ] but also for investigating protein interactions with DNA [ 53 – 55 ], peptides [ 56 ], and other proteins [ 57 – 60 ]. CPS peak H appeared to be particularly useful for analyzing water-soluble and membrane proteins [ 11 , 61 – 65 ]. All these analyses are based on utilizing the different accessibilities of electroactive residues, which is influenced by the adsorption and/or structural stability of the given protein or its complex.…”

Section: Intrinsic Electroactivity Of Proteinsmentioning

confidence: 99%

Electrochemistry in sensing of molecular interactions of proteins and their behavior in an electric field

Vacek,

Zatloukalová,

Dorčák

et al. 2023

Microchim Acta

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Electrochemical methods can be used not only for the sensitive analysis of proteins but also for deeper research into their structure, transport functions (transfer of electrons and protons), and sensing their interactions with soft and solid surfaces. Last but not least, electrochemical tools are useful for investigating the effect of an electric field on protein structure, the direct application of electrochemical methods for controlling protein function, or the micromanipulation of supramolecular protein structures. There are many experimental arrangements (modalities), from the classic configuration that works with an electrochemical cell to miniaturized electrochemical sensors and microchip platforms. The support of computational chemistry methods which appropriately complement the interpretation framework of experimental results is also important. This text describes recent directions in electrochemical methods for the determination of proteins and briefly summarizes available methodologies for the selective labeling of proteins using redox-active probes. Attention is also paid to the theoretical aspects of electron transport and the effect of an external electric field on the structure of selected proteins. Instead of providing a comprehensive overview, we aim to highlight areas of interest that have not been summarized recently, but, at the same time, represent current trends in the field. Graphical abstract

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Section: Intrinsic Electroactivity Of Proteinsmentioning

confidence: 99%

Electrochemistry in sensing of molecular interactions of proteins and their behavior in an electric field

Vacek,

Zatloukalová,

Dorčák

et al. 2023

Microchim Acta

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“…Oxidative stress denotes the imbalance between the concentration of free radicals resulting from metabolic reactions and the organisms’ ability to neutralize these radicals and has a significant role in the aging process and in the pathophysiology of age-related diseases. This imbalance is usually caused by exogenous factors such as exposure to medical treatment, ionizing radiation, presence of foreign bodies in the organism, and so forth, and affects the normal biological processes, and all cellular components, including lipids, DNA and proteins, leading to medical anomalies. , Referring strictly to proteins, their interaction with free radicals leads to oxidative lesions, among which carbonylation severely affect biological normal functions. − Consequently the carbonyl groups in oxidized proteins turn into a biomarker of oxidative stress. − Taking into account the fact that protein carbonylation is a generic term, which also describes the covalent adduction of chemical species bearing carbonyl groups, it should be highlighted that its use in this work refers strictly to the oxidative process that results in the formation of reactive ketones, aldehydes, and carbonyl groups in general.…”

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confidence: 99%

Electrochemical Sensor for Carbonyl Groups in Oxidized Proteins

2018

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The interaction of proteins with free radicals leads, among other types of damages, to the production of stable carbonyl groups, which can be used as a quantification of oxidative stress at proteins level. The aim of this study was the development of an electrochemical sensor for the detection of carbonyl groups in proteins oxidized by reactive oxygen species. Its working principle is based on the redox properties of dinitrophenylhydrazine (DNPH). BSA was used as a model protein and its oxidation achieved through Fenton reactions. Using differential pulse voltammetry at glassy carbon electrode, the electrochemical behavior of DNPH and of the native and oxidized BSA was investigated in solution. It has been shown that the hydrazine moiety of the DNPH is the electroactive center and is responsible for carbonyl complexation. Special attention was paid to the immobilization of the DNPH in order to retain its redox properties, and this was achieved on a mixed 4-styrenesulfonic acid-nafion matrix. The sensor’s surface characterization and the detection of carbonyl groups in oxidized protein were performed by voltammetry, Fourier-transformed infrared spectroscopy and scanning electron microscopy while the voltammetric results were confirmed by surface plasmon resonance measurements. It has been shown that upon interaction with carbonyl groups of the oxidized protein, the oxidation peak of the hydrazine moiety of DNPH decreases as a function of incubation time and protein concentration. The sensor sensitivity was 0.015 nmol carbonyl per mg of oxidized protein and detection limits of 50 μg oxidized BSA and 0.75 pmol carbonyls.

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