A functionalization method for the specific and selective immobilization of the streptavidin (SA) protein on semiconductor nanowires (NWs) was developed. Silicon (Si) and silicon carbide (SiC) NWs were functionalized with 3-aminopropyltriethoxysilane (APTES) and subsequently biotinylated for the conjugation of SA. Existence of a thin native oxide shell on both Si and SiC NWs enabled efficient binding of APTES with the successive attachment of biotin and SA as was confirmed with x-ray photoelectron spectroscopy, high-resolution transmission electron microscopy, and atomic force microscopy. Fluorescence microscopy demonstrated nonspecific, electrostatic binding of the SA and the bovine serum albumin (BSA) proteins to APTES-coated NWs. Inhibition of nonspecific BSA binding and enhancement of selective SA binding were achieved on biotinylated NWs. The biofunctionalized NWs have the potential to be used as biosensing platforms for the specific and selective detection of proteins.

Be, S, Si, and Ne implantations were performed at room temperature into InSb layers grown on undoped semi-insulating GaAs substrates. The implant damage in InSb is of ntype behavior. The implanted material was subjected to both isochronal and isothermal annealing schemes using a molybdenum strip heater. A maximum p-type activation of 90 % and si-type activation of 16 % was achieved for Be and S implants, respectively. Si implant has an amphoteric doping behavior.