Fig. 5: The mechanism underlying the formation of the core-shell structure.

a Chemical structure of the peptides WRWW, W_(OH)RW_(OH)W_(OH), W_(DHT)RW_(DHT)W_(DHT), YRYY. b The confocal and fast FLIM images of the peptides W_(OH)RW_(OH)W_(OH), W_(DHT)RW_(DHT)W_(DHT), YRYY with fluorophore SBD. c Backbone structure of the ordered core used for MD simulations, adapted from the configuration of 1-KMe₃ fiber⁵⁷. d Multiscale simulation scheme. The initial structure of the all-atom simulation (right) was prepared using the MARTINI simulation (left). The color coding is consistent across panels d, e, and f: core peptides (red), shell peptides (black), and water (blue). e Average peptide density profile for the last 250 ns of the simulation in a basic environment. f Average density profile of WRWW, YRYY, and WRWW (without shell) across different simulation time windows. g Initial configuration used in simulations to probe the formation process of core-shell structures. These simulations include 14 replicas of beta-strands, each represented in distinct colors, embedded within a condensate composed of individual tetrapeptides, which are depicted in gray. h Representative beta-strand structures for WRWW and YRYY before and after simulation. i Mean RMSD of beta-strands as the simulation progresses, with shaded areas indicating the standard deviation of RMSD calculated from 14 replicas. j Number of peptides in the largest clusters for WRWW and YRYY along the simulation. Source data are provided as a Source Data file.