Abstract

Protein corona refers to the structure composed of biomolecules adsorbed on the surface of nanomaterials. The study on the effect of the interaction between protein and nanoparticles can provide an important guide for the application of nanodrug delivery. To provide a reference for the research on fullerene (C60) nanocomplex drug delivery systems, this work studied the interaction between C60 nanocomplex and a variety of plasma proteins. Research showed that the protein binding with C60 nanocomplex did not change the charge properties of protein. The proteins induced the aggregation of C60 nanocomplex. The circular dichroism spectra showed that the secondary structure of the proteins changed after binding to C60 nanocomplex. The ultraviolet–visible spectra showed that the effect of C60 nanocomplex on proteins was concentration-dependent. The fluorescence spectra showed that C60 nanocomplex could intrinsic fluorescence alteration of proteins. The adsorption capacity of C60 nanocomplex to proteins was changed at 0 h and 4 h. The interaction between nanocomplex and proteins might affect the morphological characteristics of nanocomplex and the conformation of proteins. This work could provide a reference for the research and development of C60 nanocomplex and other carbon-based nanocomplex as nanoparticulate drug delivery systems.

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