The gelator was first dissolved in alkaline phosphate buffer, thanks to repulsion between negative charges in its anionic form. Subsequent pH lowering to neutral triggered amyloid fibrillation of the zwitterion in samples as diluted as 0.050 % wt. When the concentration was increased to 0.67 % wt. a self-supportive hydrogel was obtained, in contrast with the L-analog (see ESI Sections S8-S9). Interestingly, no cytotoxicity was found for the heterochiral peptide gel in live/dead assays on fibroblast cells (see ESI Section S10). Furthermore, the gel was highly resistant to protease digestion. Despite the presence of one natural peptide bond in the building block, the hydrogel was nearly unaltered after 24h of treatment with a large excess of enzyme (see ESI Section S11). Interestingly, the amyloid assembly contributed to such resistance, since the majority of the tetrapeptide in solution was digested within a few hours. We infer that the amyloid structure displays dry regions of phenylalanine zippers[5b, 15] that reduce contact with water and thus provide protection against enzymatic hydrolysis. Transmission Electron Microscopy (TEM) and Atomic Force Microscopy (AFM) investigations revealed bundles of fibrils spanning the microscale in length (Fig. ). Heating up to 363 K was required to disassemble the stable supramolecular arrangement. Instead of dissolution, as typically observed for short peptide gels, an irreversible transition to plates occurred (Fig. ). Differential scanning calorimetry (DSC) confirmed the stability of the sample up to an endothermic transition at Tm = 362 K (see ESI Fig. ).