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

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

Článek WoS

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.

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.

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

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

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

2013

01.02.2012

1452-3981

International Journal of Electrochemical Science

7

2

Srbská republika

928

942

15