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Fig. 10 | Microbial Cell Factories

Fig. 10

From: Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria

Fig. 10

Aggregation kinetics of PrPWT. The aggregation reactions of 0.5 mg/mL of purified and refolded rPrPWT were carried out under constant agitation at 600 RPM and 37 °C. In vitro preformed fibrils (2 %) or PrPs IBs (final OD350 = 0.1) were used for seeding and cross-seeding assays. PrP fibrilization (black line) as a function of time, exhibits a typical nucleation-elongation profile. The lag phase is reduced in the presence of pre-aggregated homologous protein, either PrPWT fibrils (blue line) or PrPWT IBs (red line). Cross-seeding with PrP90–231 IBs (green line) did not affect the fibrilization extent and kinetics

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