Publication detail

Electrochemical behaviour of Native and Denatured B-Sheet Breaker Prion Protein

ŠOBROVÁ, P. RYVOLOVÁ, M. HYNEK, D. ADAM, V. HUBÁLEK, J. KIZEK, R.

Original Title

Electrochemical behaviour of Native and Denatured B-Sheet Breaker Prion Protein

English Title

Electrochemical behaviour of Native and Denatured B-Sheet Breaker Prion Protein

Type

journal article in Web of Science

Language

en

Original Abstract

Prion diseases are fatal neurodegenerative and infectious disorders of humans and animals, characterized by structural transition of the host-encoded cellular prion protein (PrPC) into the aberrantly folded pathologic isoform PrPSc. The conformation change, from the a-helix in the natural protein form (PrPc) to the b-sheet of the modified protein form (PrPSc), significantly influence the protein function. The mutated form (PrPSc) is extremely resistant to the cell degradation processes and may bind other PrPc molecules inducing the conformation change to the PrPSc. The insufficiency of the physiological PrPc and toxic incidence of PrPSc participate on the genesis of prion neurodegenerative diseases. The main aim of this study was to suggest electrochemical methods for detection of b-sheet breaker prion protein. For this purpose cyclic voltammetry (CV), differential pulse voltammetry (DPV), differential pulse voltammetry Brdicka reaction and chronopotentiometric stripping analysis (CPSA) were used. Primarily, the basic electrochemical behaviour of prion and its redox system was observed using CV where 3 various peaks at potential -0.5 V (peak 1), -1.2 V (peak 2) and -1.8 V (peak 3) were detected. Under the optimal conditions (phosphate buffer, pH 7.38 and time of accumulation 100 s), detected by DPV prion was characterized using different techniques and their limits of detection were found. Adsorptive transfer stripping technique coupled with the abovementioned methods offers very lower detection limits.

English abstract

Prion diseases are fatal neurodegenerative and infectious disorders of humans and animals, characterized by structural transition of the host-encoded cellular prion protein (PrPC) into the aberrantly folded pathologic isoform PrPSc. The conformation change, from the a-helix in the natural protein form (PrPc) to the b-sheet of the modified protein form (PrPSc), significantly influence the protein function. The mutated form (PrPSc) is extremely resistant to the cell degradation processes and may bind other PrPc molecules inducing the conformation change to the PrPSc. The insufficiency of the physiological PrPc and toxic incidence of PrPSc participate on the genesis of prion neurodegenerative diseases. The main aim of this study was to suggest electrochemical methods for detection of b-sheet breaker prion protein. For this purpose cyclic voltammetry (CV), differential pulse voltammetry (DPV), differential pulse voltammetry Brdicka reaction and chronopotentiometric stripping analysis (CPSA) were used. Primarily, the basic electrochemical behaviour of prion and its redox system was observed using CV where 3 various peaks at potential -0.5 V (peak 1), -1.2 V (peak 2) and -1.8 V (peak 3) were detected. Under the optimal conditions (phosphate buffer, pH 7.38 and time of accumulation 100 s), detected by DPV prion was characterized using different techniques and their limits of detection were found. Adsorptive transfer stripping technique coupled with the abovementioned methods offers very lower detection limits.

Keywords

Prion protein (PrPSc – scrapie); Adsorptive transfer stripping technique; cyclic voltammetry (CV); differential pulse voltammetry (DPV); Brdicka reaction; Chronopotenciometric stripping analysis (CPSA)

RIV year

2012

Released

01.02.2012

Pages from

928

Pages to

942

Pages count

15

Documents

BibTex


@article{BUT92995,
  author="Pavlína {Adam} and Markéta {Vaculovičová} and David {Hynek} and Vojtěch {Adam} and Jaromír {Hubálek} and René {Kizek}",
  title="Electrochemical behaviour of Native and Denatured B-Sheet Breaker Prion Protein",
  annote="Prion diseases are fatal neurodegenerative and infectious disorders of humans and animals, characterized by structural transition of the host-encoded cellular prion protein (PrPC) into the aberrantly folded pathologic isoform PrPSc. The conformation change, from the a-helix in the natural protein form (PrPc) to the b-sheet of the modified protein form (PrPSc), significantly influence the protein function. The mutated form (PrPSc) is extremely resistant to the cell degradation processes and may bind other PrPc molecules inducing the conformation change to the PrPSc. The insufficiency of the physiological PrPc and toxic incidence of PrPSc participate on the genesis of prion neurodegenerative diseases. The main aim of this study was to suggest electrochemical methods for detection of b-sheet breaker prion protein. For this purpose cyclic voltammetry (CV), differential pulse voltammetry (DPV), differential pulse voltammetry Brdicka reaction and chronopotentiometric stripping analysis (CPSA) were used. Primarily, the basic electrochemical behaviour of prion and its redox system was observed using CV where 3 various peaks at potential -0.5 V (peak 1), -1.2 V (peak 2) and -1.8 V (peak 3) were detected. Under the optimal conditions (phosphate buffer, pH 7.38 and time of accumulation 100 s), detected by DPV prion was characterized using different techniques and their limits of detection were found. Adsorptive transfer stripping technique coupled with the abovementioned methods offers very lower detection limits.",
  chapter="92995",
  number="2",
  volume="7",
  year="2012",
  month="february",
  pages="928--942",
  type="journal article in Web of Science"
}