Quantitative and label-free technique for measuring protease activity and inhibition using a microfluidic cantilever array.

Nano Letters
Digvijay RaoraneArun Majumdar

Abstract

We report the use of a SiN x based gold coated microcantilever array to quantitatively measure the activity and inhibition of a model protease immobilized on its surface. Trypsin was covalently bound to the gold surface of the microcantilever using a synthetic spacer, and the remaining exposed silicon nitride surface was passivated with silanated polyethylene glycol. The nanoscale cantilever motions induced by trypsin during substrate turnover were quantitatively measured using an optical laser-deflection technique. These microcantilever deflections directly correlated with the degree of protease turnover of excess synthetic fibronectin substrate ( K M = 0.58 x 10 (-6) M). Inhibition of surface-immobilized trypsin by soybean trypsin inhibitor (SBTI) was also observed using this system.

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Citations

Aug 21, 2013·Biosensors & Bioelectronics·Shengbo SangGang Li
Feb 1, 2014·Biosensors & Bioelectronics·Xiaojing BaiJilin Tang
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Feb 15, 2011·Nano Letters·Genki YoshikawaHeinrich Rohrer

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