Figure 4.
Figure 4. Characterization of Affimer interaction with fibrinogen and fibrin. Binding affinities of Affimers F5 and G2 to fibrinogen were studied using ELISA-based binding assay in which increasing concentrations of the Affimers were added to fibrinogen coated wells before detection of Affimer. (A) Binding of Affimer proteins F5 and (B) G2 to fibrinogen. (C-D) Binding kinetics of Affimer F5 and G2 interaction with fibrinogen and (E-F) fibrin using Biacore SPR. Affimer proteins (12.5-800 nM) were injected over a fibrinogen- or fibrin-derivatized surface before following complex dissociation. Three independent experiments were performed to determine KD values and kinetics. Representative binding data are shown.

Characterization of Affimer interaction with fibrinogen and fibrin. Binding affinities of Affimers F5 and G2 to fibrinogen were studied using ELISA-based binding assay in which increasing concentrations of the Affimers were added to fibrinogen coated wells before detection of Affimer. (A) Binding of Affimer proteins F5 and (B) G2 to fibrinogen. (C-D) Binding kinetics of Affimer F5 and G2 interaction with fibrinogen and (E-F) fibrin using Biacore SPR. Affimer proteins (12.5-800 nM) were injected over a fibrinogen- or fibrin-derivatized surface before following complex dissociation. Three independent experiments were performed to determine KD values and kinetics. Representative binding data are shown.

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