Short Phe-rich oligopeptides, consisting of only four and five amino acids, worked as effective supramolecular hydrogelators for buffer solutions at low gelator concentrations (0.51.5 wt %). Among 10 different oligopeptides synthesized, peptide P1 (AcPhePhePheGlyLys) showed high gelation ability. Transmission electron microscopy observations suggested that the peptide molecules self-assembled into nanofibrous networks, which turned into gels. The hydrogel of peptide P1 showed reversible thermal gelsol transition and viscoelastic properties typical of a gel. Circular dichroism spectra revealed that peptide P1 formed a beta-sheetlike structure, which decreased with increasing temperature. The self-assembly of peptide P1 occurred even in the presence of nutrients in culture media and common surfactants. Escherichia coli and yeast successfully grew on the hydrogel. The hydrogel exhibited low cytotoxicity to animal cells. Finally, we demonstrated that functional compounds can be released from the hydrogel in different manners based on the interaction between the compounds and the hydrogel.