Fig. 4: Structure-activity relationship study of the Cp40-C3b interaction. | Nature Communications

Fig. 4: Structure-activity relationship study of the Cp40-C3b interaction.

From: Insight into mode-of-action and structural determinants of the compstatin family of clinical complement inhibitors

Fig. 4

a Amino acid substitutions introduced for the study, with residues altered during lead optimization steps framed in red and charged residues in green. b Localization of the changed residues on the crystal structure of Cp40 with C3b color coded as in a. SPR sensorgrams of Cp40 and its site-specifically mutated derivatives affecting the c optimized or d charged residues. Representative sensorgrams from at least three independent SPR experiments with comparable outcome. Average values and standard deviations are shown in Table 1. e Quantitative comparison of changes in binding affinities based on the results in Table 1. The overall affinity difference between Cp01 and Cp40 (i.e., 300-fold) is not shown due to scaling ranges. RU resonance units.

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