Self-sorting in functionalized
dipeptide systems can be driven by the chirality of a single amino
acid, both at a high pH in the micellar state and at a low pH in the
gel state. The structures formed are affected to some degree by the
relative concentrations of each component showing the complexity of
such an approach. The structures underpinning the gel network are
predefined by the micellar structures at a high pH. Here, we describe
the systems prepared from two dipeptide-based gelators that differ
only by the chirality of one of the amino acids. We provide firm evidence
for self-sorting in the micellar and gel phases using small-angle
neutron scattering and cryo-transmission electron microscopy (cryo-TEM),
showing that complete self-sorting occurs across a range of relative
concentrations.