We demonstrate a scattering-type scanning near-field optical microscope (s-SNOM) with broadband THz illumination. A cantilevered W tip is used in tapping AFM mode. The direct scattering spectrum is obtained and optimized by asynchronous optical sampling (ASOPS), while near-field scattering is observed by using a space-domain delay stage and harmonic demodulation of the detector signal. True near-field interaction is determined from the approach behavior of the tip to Au samples. Scattering spectra of differently doped Si are presented.
Nano-spectroscopy in the terahertz frequency range remains challenging despite recent technological progress in developing both THz emitter sources and near-field optical microscopy (SNOM). Here, we combine scattering-type SNOM with a free-electron laser light source, to tune into the 1.3–8.5 THz range. A significant portion of this range, namely, the frequencies above ∼3 THz, is not covered by previously reported near-field microscopy systems. However, it constitutes an indispensable regime where many elementary processes in solids including collective lattice excitations, charge, and spin transport occur. Our approach of nano-spectroscopy and nano-imaging provides a versatile analysis of nanostructures as small as 50 nm, hence beating the optical diffraction limit by λ/4600.
Enzyme-modified field-effect transistors (EnFETs) were prepared by immobilization of penicillinase on AlGaN∕GaN solution gate field-effect transistors. The influence of the immobilization process on enzyme functionality was analyzed by comparing covalent immobilization and physisorption. Covalent immobilization by Schiff base formation on GaN surfaces modified with an aminopropyltriethoxysilane monolayer exhibits high reproducibility with respect to the enzyme/substrate affinity. Reductive amination of the Schiff base bonds to secondary amines significantly increases the stability of the enzyme layer. Electronic characterization of the EnFET response to penicillin G indicates that covalent immobilization leads to the formation of an enzyme (sub)monolayer.
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