Kinetic parameters extracted from fitting the binding curves of concentration series of three different mAbs against a single preparation of immobilized CXCR4 ACMs.

[a]<p>KD for 12G5 binding to CXCR4-ACMS shown in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0110847#pone-0110847-g002" target="_blank">Figure 2</a> was 60.2±17 nM.</p><p>Kinetic parameters extracted from fitting the binding curves of concentration series of three different mAbs against a single preparation of immobilized CXCR4 ACMs.</p

Sensorgrams of mAb 12G5 binding (100 nM) to CXCR4-ACMs immobilized at low RU (ca. 1400) via biotin/spteptavidin immobilization of the embedding polymersome matrix.

<p>The analyte was injected in triplicate, at cycle 7, 14, and 21. Intermediate cycles involved blank injections. The blue line shows the fit to the curve assuming 1∶1 binding kinetics. The inset shows the relative decrease in binding activity of the surface as measured by the binding level 4 s before the end of the injection.</p

Kinetic screening of 12G5 mAb binding to CXCR4-ACMs immobilized onto biosensor chips.

<p>A: Ab was injected at increasing concentrations (6.25–400 nM) over 100 s, followed by a buffer wash (without regeneration) between injections (immobilization level: ca. 5000 RU; biotin/streptavidin immobilization). B. Saturation binding of 125-I SDF1α to CXCR4-ACMs. A dissociation constant of 8.4 nM was determined. C. The same series of measurements as shown in Fig. 2 A, conducted using immobilized VLPS (immobilization level: 5000 RU).</p