No abstract

No abstract

The attachment and interactions of analyte receptor biomolecules at solid-liquid interfaces are critical to development of hybrid biological-synthetic sensor devices across all size regimes. We use protein engineering approaches to engineer the sensing interface of biochemically modified field effect transistor sensors (BioFET). To date, we have deposited analyte receptor proteins on FET sensing channels by direct adsorption, used selfassembled monolayers to tether receptor proteins to planar FET SiO 2 sensing gates and demonstrated interface biochemical function and electrical function of the corresponding sensors. We have also used phage display to identify short peptides that recognize thermally grown SiO 2 . Our interest in these peptides is as affinity domains that can be inserted as translational fusions into receptor proteins (antibody fragments or other molecules) to drive oriented interaction with FET sensing surfaces. We have also identified single-chain fragment variables (scFvs, antibody fragments) that recognize an analyte of interest as potential sensor receptors. In addition, we have developed a protein engineering technology (scanning circular permutagenesis) that allows us to alter protein topography to manipulate the position of functional domains of the protein relative to the BioFET sensing surface.

Protein detection using biologically or immunologically modified field-effect transistors (bio/immunoFETs) depends on the nanoscale structure of the polymer/protein film at sensor interfaces (Bhushan 2010 Springer Handbook of Nanotechnology 3rd edn (Heidelberg: Springer); Gupta et al 2010 The effect of interface modification on bioFET sensitivity, submitted). AlGaN-based HFETs (heterojunction FETs) are attractive platforms for many protein sensing applications due to their electrical stability in high osmolarity aqueous environments and favourable current drive capabilities. However, interfacial polymer/protein films on AlGaN, though critical to HFET protein sensor function, have not yet been fully characterized. These interfacial films are typically comprised of protein–polymer films, in which analyte-specific receptors are tethered to the sensing surface with a heterobifunctional linker molecule (often a silane molecule). Here we provide insight into the structure and tribology of silane interfaces composed of one of two different silane monomers deposited on oxidized AlGaN, and other metal oxide surfaces. We demonstrate distinct morphologies and wear properties for the interfacial films, attributable to the specific chemistries of the silane monomers used in the films. For each specific silane monomer, film morphologies and wear are broadly consistent on multiple oxide surfaces. Differences in interfacial film morphology also drive improvements in sensitivity of the underlying HFET (coincident with, though not necessarily caused by, differences in interfacial film thickness). We present a testable model of the hypothetical differential interfacial depth distribution of protein analytes on FET sensor interfaces with distinct morphologies. Empirical validation of this model may rationalize the actual behaviour of planar immunoFETs, which has been shown to be contrary to expectations of bio/immunoFET behaviour prevalent in the literature for the last 20 years. Improved interfacial properties of bio/immunoHFETs have improved bio/immunoHFET performance: better understanding of interfaces may lead to mechanistic understanding of FET sensor properties and to clinical translation of the immunoFET platform.