Protein Binding by Functionalized Multiwalled Carbon Nanotubes Is Governed by the Surface Chemistry of Both Parties and the Nanotube Diameter

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Abstract

The protein binding propensity of nanoparticles determines their in vivo toxicity and their fate to be opsonized and cleared by human defense systems. In this work, protein-binding mechanisms of pristine and functionalized multiwalled carbon nanotubes (f-MWNTs) were investigated by varying f-MWNTs' diameters, nanotube surface chemistry, and proteins using steady-state and time-resolved fluorescence, and circular dichroism (CD) spectroscopies. The f-MWNTs with a larger diameter (∼40 nm) generally exhibited stronger protein binding compared to those with a smaller diameter (∼10 nm), demonstrating that the curvature of nanoparticles plays a key role in determining the protein binding affinity. Negative charges or steric properties on f-MWNTs enhanced binding for some proteins but not others, indicating that the electrostatic and stereochemical nature of both nanotubes and proteins govern nanotube/protein binding. Protein fluorescence lifetime was not altered by the binding while the intensity was quenched indicating a static quenching through complex formation. The binding-induced conformational changes were further confirmed by CD studies.

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