Amyloid assembly and disassembly have attracted great interest in recent years, with Fmoc-derived gelators having gained wide popularity. By contrast, mastering the supramolecular behavior of short peptides devoid of synthetic appendages, which are more relevant to natural processes, is still very challenging. On one hand, amyloid disassembly could be of high value in a therapeutic context, yet fibril re-assembly is unavoidable when it is the thermodynamic product. On the other hand, general rules for the design of building blocks of three or four unprotected amino acids (aa) that self-organize into macroscopicand ideally functional -hydrogels, as opposed to insoluble aggregates, are not yet fully elucidated, although integration of experiments with computational tools is enabling fast progress in the field. It is well-established that amyloids have an amphipathic nature. Hydrophobic components segregate in steric zippers that exclude water and stabilize the structure. In particular, phenylalanine (Phe)-based zippers have been reported for minimalistic peptides.[5] Yet, hydrophilic components must favorably interact with water to yield a bulk hydrogel. Gel-to-sol transition can be conveniently induced by heating, and usually the gel reforms upon cooling to rt. Reported examples of unprotected gelling peptides as short as three or four residues indeed display such thermo-reversible behavior.