Changes of electrocatalytic response of bovine serum albumin after its methylation and acetylation

Ostatná, Veronika; Kasalová, Veronika; Kmeťová, Katarína; Šedo, Ondřej

doi:10.1016/j.jelechem.2017.11.044

Cited by 9 publications

(3 citation statements)

References 50 publications

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“…We suppose that completely different behavior of histone H3 can be due to its posttranslational modification. Similar behavior at charged interface was described previously for acetylated BSA . Probably electroactive residues of H3 histone, such as Lys and Arg, were involved in the modification and therefore this histone was very weakly electroactive in contrast to other proteins.…”

Section: Comparison Of Individual Amino Acid (Aa) Content In Selectedmentioning

confidence: 99%

Chronopotentiometric Analysis of Proteins at Charged Electrode Surfaces

et al. 2019

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Protein properties and functions are strongly dependent on the structure and amino acid content. In this work, catalytic hydrogen evolution reaction (CHER) of five proteins (human serum albumin, lysozyme, β‐synuclein, H2 A and H3 histones) were studied using constant current chronopotentiometric stripping (CPS) with the aim to find out the association between protein content and its electrochemical response. We have shown that the height and potential of CPS peak H in dependence on accumulation potential differed for the studied proteins, while the CPS peak area was almost the same for all of them. CV and CPS peaks H of Cys‐containing proteins appeared at less negative potentials in comparison to proteins without Cys, suggesting easier CHER. Acidic and basic proteins not containing Cys can be also recognized due to their different CPS response after their adsorption at the positive and negative charged interface.

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Section: Comparison Of Individual Amino Acid (Aa) Content In Selectedmentioning

confidence: 99%

Chronopotentiometric Analysis of Proteins at Charged Electrode Surfaces

et al. 2019

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“…The denaturation of surface-attached proteins can be minimized by adjusting the duration of the protein exposure to the electric field to milliseconds [ 39 ], as well as other experimental conditions, such as solution temperature [ 37 ] and ionic strength [ 40 ]. 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 ].…”

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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“…The CPS signal of a protein was denominated as “peak H” and its appearing in the protein analysis is a result of catalytic hydrogen evolution reaction (CHER) of amino acids residues bearing exchangeable proton, such as Cys, Arg, Lys, and His . Global and local changes in the protein structure such as denaturation , mutation , chemical modification , damage , redox state , and aggregation can be studied using CPS due to susceptibility of proteins to effects of electric field. In the course of chronopotentiogram recording, the electrode potential shifts slower during an electrode process than in its absence, when potential changes can reach extremely high rates.…”

Section: Introductionmentioning

confidence: 99%

BSA‐Polysaccharide Interactions at Negatively Charged Electrode Surface. Effects of Current Density.

et al. 2019

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Constant current chronopotentiometric stripping (CPS) peak H due to catalytic hydrogen evolution reaction on Hg‐containing electrodes appeared useful in the analysis of protein complexes with single‐stranded and double‐stranded DNA as well as with peptides. In dependence on stripping current (Istr), structural transition of the protein alone or in complexes can be followed as a result of the protein exposure to electric field effects. For the first time we show here that the CPS analysis can be used for the study of the interaction of BSA with a polysaccharide namely sodium alginate (SA). BSA‐SA complex formation was accompanied by the shift of the structural transition of BSA to lower ‐Istr intensities. Another polysaccharide dextran did not alter Istr‐dependent structural transition of BSA. BSA‐SA complex can be disturbed by an electric field effect or high ionic strength confirming the electrostatic nature of BSA‐SA interaction.

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Changes of electrocatalytic response of bovine serum albumin after its methylation and acetylation

Cited by 9 publications

References 50 publications

Chronopotentiometric Analysis of Proteins at Charged Electrode Surfaces

Chronopotentiometric Analysis of Proteins at Charged Electrode Surfaces

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

BSA‐Polysaccharide Interactions at Negatively Charged Electrode Surface. Effects of Current Density.

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