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.

• Klíčová slova
• Electrode, Microdevice, Peptide, Protein, Sensor,
• MeSH
• elektrochemické techniky * metody   MeSH
• elektrochemie MeSH
• oxidace-redukce MeSH
• proteiny * MeSH
• transport elektronů MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• přehledy MeSH
• Názvy látek
• proteiny * MeSH

In recent decades, it has become clear that most of human proteins are glycosylated and that protein glycosylation plays an important role in health and diseases. At present, simple, fast and inexpensive methods are sought for clinical applications and particularly for improved diagnostics of various diseases, including cancer. We propose a label- and reagent-free electrochemical method based on chronopotentiometric stripping (CPS) analysis and a hanging mercury drop electrode for the detection of interaction of sialylated protein biomarker a prostate specific antigen (PSA) with two important lectins: Sambucus nigra agglutinin (SNA) and Maackia amurensis agglutinin (MAA). Incubation of PSA-modified electrode with specific SNA lectin resulted in an increase of CPS peak H of the complex as compared to this peak of individual PSA. By adjusting polarization current and temperature, PSA-MAA interaction can be either eliminated or distinguished from the more abundant PSA-SNA complex. CPS data were in a good agreement with the data obtained by complementary methods, namely surface plasmon resonance and fluorescent lectin microarray. It can be anticipated that CPS will find application in glycomics and proteomics.

• Klíčová slova
• A prostate specific antigen, Chronopotentiometric analysis, Lectin-glycoprotein interaction, Mercury electrode, Sialylated glycan isomers,
• MeSH
• aglutininy metabolismus   MeSH
• bez černý chemie   MeSH
• elektrická vodivost * MeSH
• elektrochemie MeSH
• kyselina N-acetylneuraminová metabolismus   MeSH
• Maackia chemie   MeSH
• prostatický specifický antigen chemie   metabolismus   MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• aglutininy MeSH
• kyselina N-acetylneuraminová MeSH
• prostatický specifický antigen MeSH

• MeSH
• biosenzitivní techniky přístrojové vybavení   metody   MeSH
• elektrochemické techniky přístrojové vybavení   metody   MeSH
• glykomika přístrojové vybavení   metody   MeSH
• glykoproteiny analýza   metabolismus   MeSH
• lidé MeSH
• molekulární modely MeSH
• molekulární sekvence - údaje MeSH
• proteiny analýza   metabolismus   MeSH
• sacharidové sekvence MeSH
• sekvence aminokyselin MeSH
• zvířata MeSH
• Check Tag
• lidé MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• přehledy MeSH
• Názvy látek
• glykoproteiny MeSH
• proteiny MeSH