Interactions between carbon nanodots with human serum albumin and γ-globulins: The effects on the transportation function

Carbon nanodots (C-dots) have attracted great attention as a new class of luminescent nanomaterials due to their superior physical and chemical properties. In order to better understand the basic behavior of C-dots in biological systems, a series of photophysical measurements were applied to study the interactions of C-dots with human serum albumin (HSA) and γ-globulins. The fluorescence of proteins was quenched by the dynamic mechanism rather than the formation of a protein/C-dots complex. The apparent dissociation constants of the C-dots bound to HSA and γ-globulins were of the same order of magnitude. Furthermore, it is proven that C-dots showed little influence on the conformation of HSA and γ-globulins. In addition, Fourier transform infrared and fluorescence spectroscopic studies demonstrated that the interaction between C-dots and two kinds of serum proteins was driven by hydrophobic and van der waals forces. Since the bioavailability of drugs can be modulated by their interactions with proteins, the variations of binding constants of three drugs with HSA and γ-globulins in the presence of different concentrations of C-dots (0–84 μmol L−1) have also been analyzed in this work, to reflect the effect of C-dots on the transportation function of HSA and γ-globulins.