Fig. 3: FPS resolves binding kinetics of dimeric, tetrameric, and octameric peptide binders in high-throughput.

a–c FPS curves of all dimers (a, yellow), tetramers (b, red), and octamers (c, purple) tested are displayed next to the respective association levels. Peptide architecture is denoted as described in Fig. 1a). In brief, epitope length is denoted by “e” and the length of the respective PEG linker is represented by o₁, o₂ or o₃. For a complete list of the kinetic parameters of all compounds tested, refer to supplementary table 1. d Rate map of all dimers (yellow), tetramers (red), and octamers (blue) with a determinable on- and off-rate. Epitope lengths are color-coded. Note the the high dependence of dimer affinity on epitope length. 10 µM, 1 µM, and 100 nM affinities are indicated as dashed, grey lines. e Zoomed-in view of (d) with octameric binders in focus. Varying architectures are color-coded, and 100 nM affinity is indicated as dashed, grey line. Note that octamers with highest affinity contain ≥3 PEG building blocks in the outer o₁ position. Error bars represent fit uncertainty in n = 1 measurement. Source Data are provided as Supplementary Data 1.