Gallium arsenide (GaAs) is a promising candidate as a platform for optical biosensing devices due to its enabling optoelectronic properties. However, the biofunctionalisation of the GaAs surface has not received much attention compared to gold, carbon and silicon surfaces. Here we report a study presenting a physicochemical surface characterisation of the GaAs surface along the functionalisation with a high-affinity bioconjugation pair widely explored in the life sciences - biotin and neutravidin. Combined X-ray photoelectron spectroscopy (XPS), wettability measurements and spectroscopic ellipsometry were used for a reliable characterisation of the surface functionalisation process. The results suggest that a film with a thickness lower than 10 nm was formed, with a neutravidin to biotin ratio of 1:25 on the GaAs surface. Reduction of non-specific binding of the protein to the surface was achieved by optimising the protein buffer and rinsing steps. This study shows the feasibility of using GaAs as a platform for specific biomolecular recognition, paving the way to a new generation of optoelectronic biosensors.
Keywords: Alkanethiolate film; Biotin; Carbodiimide chemistry; Compound semiconductor; Contact angle; Optical biosensor; Protein non-specific binding; Self-assembled monolayer; Spectroscopic ellipsometry; X-ray photoelectron spectroscopy.
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