Fig. 4: Multimer binding prediction and inhibition potency.
From: Multivalent binding kinetics resolved by fluorescence proximity sensing
Measured KD values (a), off- (b), and on-rates (c) are plotted against predicted values in a leave-one-out cross-validation. Note the high correlation between predicted and obtained KD values. The obtained association levels are plotted against the observed KD values (d), off- (e), and on-rates (f). Note the low correlation between association levels and other kinetic parameters. g Schematic representation of µSPOT peptide microarrays, harbouring geph-binding peptides as cellulose conjugates. Native geph from mouse brain lysates was preincubated with multimeric peptides to neutralize geph-binding to on-chip peptides. h Normalized geph binding intensity to GlyR β-derived on-chip peptides in µSPOT format in the presence of varying competitor concentrations. Native geph binding to on-chip peptides was resolved by antibody detection and chemiluminescent readout. Note that tetrameric and octameric peptides effectively neutralized geph binding at lower concentrations than dimeric peptides. Data are presented as mean of n = 2 experiments. Source Data are provided as Supplementary Data 1.
