Supplementary Tables: Potassium channel blocker crafted by ɑ-hairpinin scaffold engineering

Analysis of intermolecular contacts between the channel and the peptides for all systems in dynamics.<br>H-bonds, salt bridges, stacking/π-π interactions, and cation-π interactions observed in 110 ns MD of complexes KV1.3 with Tk-hefu, Tk-hefu-2 and the analogs proposed for the computational study on the first round of modification All the contacts in the table “aligned” according to amino acid sequence alignment of the peptides. Each contact in the each complex is put in correspondence with analogous contacts in the others complexes. In case when an analogous contact was not observed during MD, the corresponding cell in the table is empty. Lifetime of each contact counted as part of MD-trajectory total time (110 ns). “s” stands for short-living contacts: lifetime is less than 10 %; “m” stands for medium-living contacts: lifetime is less then 50 %; “l” stands for long-living contacts: lifetime is greater than 50 %. Subunit identifiers (A, B, C, or D) merged with the name and number of channel residues (i.e. Gly337A).