A radio frequency based method to screen the activity of hydrolytic enzymes on native substrates is presented. The switchable activity of allosteric, hydrolytic enzymes was used as a single-input, ‘buffer’ logic gate (performing YES and NOT) in a screen-printable biosensor. The enzyme substrate functioned as an ‘AND’ logic gate with the enzyme and co-factor as inputs. These (bio)-logic materials transduced a signal by the cofactor activating the enzyme which then degraded the substrate that formed the dielectric of a tuning capacitor in an inductor-capacitor (LC) circuit. The degradation of the substrate was engineered to shift the capacitance and thus the resonant frequency of the device. The resonant frequency was monitored wirelessly with a low-power vector network analyzer observing the S21 parameter. Proof of concept is shown with subtilisin as the enzyme, activated by calcium (100 μg/ml and 5 mM respectively) degrading a collagen substrate with a demonstrated wireless read range of up to 4 cm. Selectivity over other divalent cations (magnesium, copper II, and manganese II) and the effect of receiver motion is also shown on the wireless measurement. The utility of this technique is also shown on current efforts to screen a broader panel of protease activity.<br/>

High-throughput screening of hydrolytic enzyme activity via wireless antennas with embedded (bio)-logic

253rd National Meeting (2017)

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