Publication details
INFLUENCE OF HEAT DENATURATION OF Beta-SHEET BREAKER PRION PROTEIN ON ELECTROCHEMICAL RESPONCE
| Authors | |
|---|---|
| Year of publication | 2012 |
| Type | Article in Proceedings |
| Conference | XII. Pracovní setkání fyzikálních chemiků a elektrochemiků. Sborník příspěvků. |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | prion protein;cyclic voltammetry;differential pulse voltammetry;Brdicka reaction;chronopotentiometry |
| Description | Electrochemical study of Beta-sheet breaker prion protein is the main aim of this study. For this purpose, cyclic voltammetry (CV), differential pulse voltammetry, differential pulse voltammetry Brdicka reaction and chronopotentiometric stripping analysis were used. 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. The lowest limits of detection were determined by CPSA AdTS i.e. 25 pmol in volume of 5 microl. CPSA is therefore a very sensitive tool for the studying of prion behaviour. Moreover, the influence of heat denaturation was observed. It clearly follows from the results obtained that signals of prion decreased linearly depending on the duration of the heat treatment at 99 C for various time intervals: 0, 15, 30, 45, and 60 min. The correlation coefficients of the measured dependencies as 0.9929, 0.9973, 0.9965 and 0.9957 were determined by CV, DPV, DPV Brdicka reaction and the most sensitive CPSA, respectively. |