Fig. 2. Change of hydrodynamic radius r_h of CNDs (batch #1) as recorded in phosphate-buffered saline (PBS) in dependence of the protein concentration.

a HSA; b Tf; c α2M. From the plots the fit parameters K_D, N_max, n, r_h,0, and Δr_h,max were obtained, which are listed in Table 2. K_d is the apparent dissociation constant of the CND-protein complex, N_max is the maximum number of bound proteins per CND under saturation conditions, n is the Hill coefficient, r_h,0 is the hydrodynamic radius of the CNDs without attached proteins, and Δr_h,max is the difference in effective hydrodynamic radius between CNDs saturated with proteins and CNDs without attached proteins. The shown data were obtained with batch #1. Results are shown as mean values with error bars (i.e. the corresponding standard deviations) from three independent samples (n = 3) over three independent experiments.