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. Author manuscript; available in PMC: 2018 Aug 18.
Published in final edited form as: ACS Synth Biol. 2017 May 22;6(8):1484–1495. doi: 10.1021/acssynbio.6b00392

Figure 4.

Figure 4

N-terminal fusion architecture can accommodate diverse inhibitory motifs to yield unique COVERT molecules that are specifically activated by cognate proteases. (a,b) DDDDK-GrB and ENLYFQ-GrB were purified from the supernatant of transiently transfected HEK293T cells and co-incubated with EK and TEVp, respectively. The resulting GrB activity of (a) DDDDK-GrB and (b) ENLYFQ-GrB against Ac-IEPD-pNA substrates was quantified by the rate of increase in absorbance at 405 nm. (c) GrB activity per mole of target protease (i.e. EK or TEVp) was calculated to compare the relative rate of COVERT activation. All values indicate the mean of triplicate samples and error bars represent ±1 s.d.