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. 2010 Sep 29;84(23):12236–12244. doi: 10.1128/JVI.01579-10

FIG. 4.

FIG. 4.

101F binding to RSV F glycoprotein and epitope peptide. 101F binds the RSV F glycoprotein 16,000-fold tighter than the epitope peptide, suggesting the 101F epitope is more complex than the linear region. (A) SPR sensorgram of 101F Fab binding to immobilized RSV F. Five 2-fold dilutions of 101F Fab starting at 25 nM were measured, plus a 3.125 nM duplicate. Red lines represent best fits of kinetic data to a 1:1 Langmuir binding model. (B, top) SPR sensorgram of peptide binding to immobilized 101F IgG. Six 2-fold dilutions of peptide starting at 100 μM were measured, plus a 12.5 μM duplicate. Binding kinetics were too fast to accurately determine rate constants. (Bottom) Plot of equilibrium response as a function of peptide concentration. The red line represents the best fit of the data to the single-site equilibrium binding model.