Label-free field-effect transistor-based immunosensors are promising candidates for proteomics and peptidomics-based diagnostics and therapeutics due to their high multiplexing capability, fast response time, and ability to increase the sensor sensitivity due to the short length of peptides. In this work, planar junctionless field-effect transistor sensors (FETs) were fabricated and characterized for pH sensing. The device with SiO₂ gate oxide has shown voltage sensitivity of 41.8 ± 1.4, 39.9 ± 1.4, 39.0 ± 1.1, and 37.6 ± 1.0 mV/pH for constant drain currents of 5, 10, 20, and 50 nA, respectively, with a drain to source voltage of 0.05 V. The drift analysis shows a stability over time of −18 nA/h (pH 7.75), −3.5 nA/h (pH 6.84), −0.5 nA/h (pH 4.91), 0.5 nA/h (pH 3.43), corresponding to a pH drift of −0.45, −0.09, −0.01, and 0.01 per h. Theoretical modeling and simulation resulted in a mean value of the surface states of 3.8 × 10¹⁵/cm² with a standard deviation of 3.6 × 10¹⁵/cm². We have experimentally verified the number of surface sites due to APTES, peptide, and protein immobilization, which is in line with the theoretical calculations for FETs to be used for detecting peptide-protein interactions for future applications.

In the ElectroMed project, we are interested in screening certain peptide sequences for their ability to selectively interact with antibodies or MHC proteins. This poses a combinatorial challenge that requires a highly multiplexed setup of label-free immunosensors. Label-free FET-based immunosensors are good candidates due to their high multiplexing capability and fast response time. Nanowire-based FET sensors have shown high sensitivity but are unreliable for clinical applications due to drift and gate stability issues. To address this, a label-free immuno-FET architecture based on planar junctionless FET devices is proposed. This geometry can improve the signal-to-noise ratio due to its larger planar structure, which is less prone to defects that cause noise and is better suited to the functionalization of different receptor molecules.