Calculated Kds and derived ΔG° (Gibbs free energy of binding) for the interactions between eIF4E and the hybrid eIF4G1/PHAGESOL peptides.

The table shows the peptide sequences used to study the relevance of individual amino acid changes observed in the phage derived sequence. The peptides were characterized using a fluorescence based thermal denaturation method and by using SPR with eIF4E amine coupled to the chip surface. Kds were also derived from the respective thermal shift and SPR data. Kds were derived from the equilibrium responses (Keq) and from the association and dissociation phases (Kkin) of the SPR data. The Gibbs free energy of binding (ΔG°) was calculated with the equation ΔG = −RT ln Ka using both dissociation constant values determined.