Outstanding transport characteristics and high surface-to-volume ratios are several advantages that carbon nanotubes possess that make them attractive candidates for protein immobilization matrices in biosensor applications. A further advantage of using carbon nanotubes is that their structure (e.g., diameter, length, density) can potentially be controlled during synthesis. In the present study, the effects of carbon nanotube structure on enzyme immobilization onto carbon nanotube arrays are investigated. Bovine serum albumin (BSA) serves as both a blocking agent for prevention of nonspecific adsorption and as a support for anchoring bioreceptors. BSA, a globular protein having a 4 to 6 nm characteristic dimension, is stably adsorbed through mechanisms that involve hydrophobic interactions between surfaces presented by the carbon nanotubes and the spacing between the nanotubes with the protein. Protein adsorption is confirmed by fluorescence microscopy of surfaces that have been exposed to fluourescein isothiocyanate (FITC) labeled BSA. The adsorption of biotinylated BSA can be used, through a sandwich immobilization scheme, to provide an anchor for streptavidin, which in turn has at least one other adsorption site that is specific for other biotinylated proteins such as glucose oxidase that would form a biorecognition or catalytic element in a functional biosensor. Correlation between carbon nanotube structure and protein adsorption at the nano-bio interface could eventually lead to growth conditions that yield carbon nanotubes for biosensor applications with optimal protein adsorption characteristics.

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