Figure 6
From: Molecular basis for the recognition of 24-(S)-hydroxycholesterol by integrin αvβ3
The binding affinities of 24HC and 25HC to integrin αvβ3 were determined by surface plasmon resonance (SPR). (A–B) 24HC and (C–D) 25HC. Increasing concentrations of the ligand (as indicated in the figures) were injected into both the integrin-immobilized and control blank surface of the CM5 chip, as described in “Materials and methods” Section. The analyte injection was terminated at 180 s and allowed to dissociate in the running buffer for 600 s. Representative SPR data were quantified using the steady-state equilibrium binding model to calculate the affinity constant (KD), as shown in the curve-fitting graphs.
