FIGURE 3.

Effects of chirality and reduction of cyclotides on membrane binding. A, 40 μm l-kB2 and its d-isomer were injected for 180 s over POPC/POPE (80:20) lipid surfaces deposited on an L1 chip. Dissociation was monitored for 600 s after the injection was stopped. Sensorgrams obtained show that for the same amount of lipid on the surface, d-kB2 has a lower amount of peptide bound to the membrane than its mirror image isomer. Dissociation rates are identical. B, reduced kB1 and cyO2 were tested for their membrane-binding ability to POPC/POPE (80:20) model membranes. P/L was plotted versus peptide concentration. Reduced peptides have weak binding relative to their oxidized native forms.