Fig. 5: Competitive experiments for Myc binding between small molecule inhibitors and Max.

a, b Real-time current trajectories (time resolution of 17 μs) of competition between Max and 10074-A4 (0.01× PBS, pH = 7.4, 100 μM 10074-A4, and 100 nM DQ47). a The left panel shows current data over 60 s and the right image is the current distribution histogram; b shows magnified images of the marked areas in (a). Blue, green and red represent 10074-Myc binding equilibrium, interacting folding and Myc-Max binding equilibrium. c, d Real-time current trajectories (time resolution of 17 μs) of competition between Max and PKUMDL-YC-1205 (0.01× PBS buffer, pH = 7.4, 100 μM 1205, and 100 nM DQ47). c The left panel shows current data over 60 s and the right image is the current distribution histogram; d shows magnified images of the marked areas in (c). purple, green and red represent 1205-Myc binding equilibrium, interacting folding and Myc-Max binding equilibrium. e Schematic diagram of the competition process between DQ47 and PKUMDL-YC-1205. The structures were adapted from ref. ³². Purple and light purple represent Myc binding state with 1205 and Myc* with 1205. The rest colors are defined as in Fig. 1. f The population of Myc-Max binding states at different DQ47 concentrations in the presence of 100 μM inhibitor (blue and purple represent 100 μM 10074 and 1205 solution; n = 3, number of the devices, data are presented as mean values ± SD). The apparent dissociation constants of the Myc-Max binding process in different inhibitor solutions were obtained by fitting the Hill equation (Supplementary Table 7). Source data are provided as a Source Data file.