Electrical dual-sensing method for real-time quantitative monitoring of cell-secreted MMP-9 and cellular morphology during migration process

MMP-9 (92kDa gelatinease), which is member of matrix metalloproteinases (MMPs) family, plays a crucial role in the breakdown of extracellular matrix (ECM) by degrading the major components of ECM that lead to tumor cell invasion and metastasis through the basement membrane. Our study presents the on-chip dual-sensing device for rapid detection of cell-secreted MMP-9 and corresponding cell morphology changes in real-time domain. The device consists of 2 sensing platforms (both are interdigitated array microelectrodes – IDAMs) within 1 common fluidic chamber: one detects the cell morphology responses via Electric Cell-substrate Impedance Sensing (ECIS) technique, meanwhile the other records the cleavage effect between cell-secreted MMP-9 and the surface immobilized peptide via the capacitance-based sensing method. Thanks to the selectivity of designed peptide, this approach allows the rapid and specific detection of MMP-9. In comparison with gold standard ELISA assay, the detection time was significantly reduced from over 4h to within 30min with the wide detection range from 10pM to 10nM. Finally, this study provides the novel model for MMP-9 protease direct detection from living cell and new insights in multi-purpose detection of cancer associated enzyme and cell migration behavior. •MMP-9 secretion was quantified during the motility of MCF-7 cells by dual-sensing device.•The device has different sensing platforms for cell morphology and cell-secreted protease.•MMP-9 secretion rate was defined to correspond to the morphology changes of MCF-7 cells.