Understanding the structure and function of glucose binding proteins complexed with Single Walled Carbon Nanotubes (SWNT) is important for the development of many applications, including near infrared fluorescent sensors and nanostructure particle tracking. Here-in, we utilize circular dichroism, thermal denaturation, photo-absorption spectroscopy and atomic force microscopy to study such nanostructures synthesized by conjugating glucose binding protein (GBP) to a poly vinyl alcohol (PVA) scaffold used to wrap SWNT. We find that such coupling schemes yield approximately 0.9 proteins per nanotube. The protein retains its glucose-binding activity after complexation and is thermally stable below 36 �C. Above this temperature threshold, the hydrophobic nanotube is shown to increase the denaturation, lowering the midpoint denaturation temperature (Tm) by 5 �C and 4 �C in the absence and presence of 10 mM glucose, respectively. This data highlights that using techniques such as circular dichroism spectroscopy and thermal denaturation may be necessary to fully characterize such protein-nanomaterial nanostructures.

Structure and function of glucose binding protein-single walled carbon nanotube complexes

244th National Meeting (2012)

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