Supramolecular hydrogels have attracted great interest as dynamic soft matter for a variety of potential applications, spanning from energy,1 to medicine,2 environmental remediation,3 and beyond. Their matrices are composed of non-covalent interactions that provide opportunities for their modulation, formation, and dissociation on demand using ad hoc stimuli. In particular, the inclusion of several components is becoming popular, especially for more advanced applications, where each one can play a structural and/or functional role.5 However, the detailed characterisation of such systems, especially the localisation of the different components, is not always trivial. On one hand, components of very different nature, such as metal nanostructures6-8 or nanocarbons9-12 and organic assemblies, can be easily identified by microscopy. On the other hand, organic components are far more challenging to distinguish at the nanoscale. Furthermore, hydrogels composed of similar molecules that self-organise into nanofibrillar matrices may arise from different types of assemblies, such as those composed of different gelators (i.e., coassemblies), or those composed exclusively of either gelator through a self-sorting mechanism. One convenient strategy employs gelators with pH-responsive behaviour within distinct pH ranges, and/or the use of gelators that respond to different stimuli, so that specific gelation triggers can be used to exert selective control over the organization of each gelator. Another interesting approach derives from the finding that racemic mixtures of gelators can yield coassemblies with peculiar properties, and stronger gel networks. In particular, self-assembling peptides are attractive gelators, thanks to their easy modular design and synthesis, and the possibility to include diverse amino acids, thus functional groups, chirality, properties, and functions.16 Schneider and collaborators had reported in 2011 the racemic assembly of a peptide gelator with remarkably enhanced rigidity relative to gels formed by each enantiomer alone.17 The elucidation of how the two enantiomers were interacting was very challenging, since no significant differences were found by spectroscopic or microscopic investigations. It took a few years, and an arsenal of advanced techniques, Scheme 1. Heterochiral tripeptides studied in this work for co-assembly.