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pNP-L activity was followed again to identify active fractions.
DPE-L activity is also context dependent, exerting a greater effect in constitutive than activated transcription.
For three other compounds (3, 8 and 10), ChT-L activity alone was significantly inhibited.
The best dimer inhibited CT-L activity 800-times more efficiently than the reference inhibitor.
However, even more interesting was the impact of Au-NPs on cathepsin L activity.
Cathepsin L activity appears to be more sensitive to Ag-NP exposure.
All 4 types of Ag-NPs testedemonstrateded a significant reduction of cathepsin L activity in Vero cells (Figure 3).
Alternatively, the impact of nanoparticles on cathepsin L activity depends greatly on the type and size of the material.
When the Vero cells were exposed to Au-NPs, a stimulatory effect of cathepsin L activity was observed.
Conversely, a decline in cathepsin L activity was observed when the Au-NPs were incubated with the purified enzyme.
Despite quantitative differences, SlCYS8 single variants engineered to strongly inhibit Cys proteases showed improved potency against cathepsin L activity of either population.
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