Figure 5

Theoretical determination of the optimal conditions for the Peptidomatrix. (A) Binding of the antibody (at different dilutions) to wells containing increasing amounts of peptide,0.1(●),1(○), 10(▼), 100(▽). (B) Titration of bound peptide (different amounts) with increasing concentrations of antibody, 0.1(●), 1(○), 10(▼), 100(▽). (C) Competition between attached and free peptide using 4 concentrations of attached peptide,0.1(●),1(○), 10(▼), 100(▽), first antibody 'dilution' was 10. (D) Competition between attached and free peptide using 4 concentrations of antibody 0.1(●),1(○), 10(▼), 100(▽), 'attached peptide' was 10. All these curves are simulations and were drawn using equation A2 (for panel A and B) and A5 (for panel C and D), with kinetic parameters of Ka = 30, Kp = 10, cap = 50 and Kf = 1, see the appendix for details. All the data were analyzed using the Michaelis-Menten equation (normal and descending hyperbola). The derived values of Kd and Amax appear in table 5.