Skip to main content
. Author manuscript; available in PMC: 2019 May 31.
Published in final edited form as: Biochemistry. 2017 May 2;56(19):2518–2528. doi: 10.1021/acs.biochem.7b00087

Figure 4.

Figure 4.

SPR-detected interaction between the (β15–66)2 and VLDLR(1–8) fragments at different concentrations of NaCl, 0.15 M (A), 0.2 M (B), 0.25 (C), and 0.3 M (D). The (β15–66)2 fragment at increasing concentrations, 0.25, 0.5, 1, 2.5 and 5 nM (A), 0.5, 1, 2.5, 5 and 10 nM (B), and 1, 2.5, 5, 10, and 25 (C and D), was added to the immobilized VLDLR(1–8) fragment and its association/dissociation was monitored in real time while registering the resonance signal (response) using BIAcore biosensor. The dotted curves represent the best fit of the binding data using global fitting analysis (see Materials and Methods); the determined Kd values are presented in Table 2. (E) Debye-Huckel plots for binding of VLDLR(1–8) to (β15–66)2 at different ionic strengths. The Kd values were taken from SPR data presented in panels A-D and Table 2, and the log10Kd values represent an average of at least three independent experiments ± SD; a slope of 5.2 ± 0.2 was determined by linear regression analysis.