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Electrochemical and optical study of metallothionein interactions with prion proteins
A. Cardova, P. Adam, S. Mariani, L. Richtera, Z. Heger, J. Labuda, M. Minunni, V. Adam,
Jazyk angličtina Země Velká Británie
Typ dokumentu časopisecké články
Grantová podpora
NV15-28334A
MZ0
CEP - Centrální evidence projektů
- MeSH
- elektrochemické techniky * MeSH
- měď MeSH
- metalothionein MeSH
- prionová bílkovina MeSH
- Publikační typ
- časopisecké články MeSH
The prion protein (PrPC) can be structurally shifted to its PrPScisoform causing a wide range of neurodegenerative diseases, which are currently incurable. There is an evidence that metallothioneins (MTs), and especially MT-3, are associated with neurodegenerative diseases. PrPCand MTs play pivotal roles in maintaining metal homeostasis; therefore, it is conceivable that each of them has its own significance in prion diseases. In this paper, we study the nature of interactions between PrPC, MT, and copper ions, Cu(II), using the method of differential pulse voltammetry (DPV) coupled with adsorptive transfer stripping technique (AdTS). Electrochemical properties of PrP itself and its interactions with both the Cu(II) ions and MTs have been found. Based on the results obtained, we hypothesised the formation of the complex in molar ratio 2:1 (PrPC:MT). Surface plasmon resonance imaging (SPRi) was used as a control reference assay to further confirm results obtained by the electrochemical approach, such as the specific interactions between PrPCand MT-3.
Central European Institute of Technology Brno University of Technology Brno Czech Republic
Department of Chemistry and Biochemistry Mendel University in Brno Brno Czech Republic
Department of Veterinary Medicine University of Cambridge UK
Dipartimento di Chimica Ugo Schiff and CSGI Università di Firenze Sesto Fiorentino Italy
Citace poskytuje Crossref.org
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- $a Cardova, Alzbeta $u Department of Chemistry and Biochemistry, Mendel University in Brno, Brno, Czech Republic; Department of Veterinary Medicine, University of Cambridge, UK.
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- $a Electrochemical and optical study of metallothionein interactions with prion proteins / $c A. Cardova, P. Adam, S. Mariani, L. Richtera, Z. Heger, J. Labuda, M. Minunni, V. Adam,
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- $a The prion protein (PrPC) can be structurally shifted to its PrPScisoform causing a wide range of neurodegenerative diseases, which are currently incurable. There is an evidence that metallothioneins (MTs), and especially MT-3, are associated with neurodegenerative diseases. PrPCand MTs play pivotal roles in maintaining metal homeostasis; therefore, it is conceivable that each of them has its own significance in prion diseases. In this paper, we study the nature of interactions between PrPC, MT, and copper ions, Cu(II), using the method of differential pulse voltammetry (DPV) coupled with adsorptive transfer stripping technique (AdTS). Electrochemical properties of PrP itself and its interactions with both the Cu(II) ions and MTs have been found. Based on the results obtained, we hypothesised the formation of the complex in molar ratio 2:1 (PrPC:MT). Surface plasmon resonance imaging (SPRi) was used as a control reference assay to further confirm results obtained by the electrochemical approach, such as the specific interactions between PrPCand MT-3.
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- $a Adam, Pavlina $u Department of Chemistry and Biochemistry, Mendel University in Brno, Brno, Czech Republic; Central European Institute of Technology, Brno University of Technology, Brno, Czech Republic.
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