An amphiphilic peptide designed with serine as a polar residue showed gelation in both water and organic solvents. This sequential peptide has a strong tendency to adopt beta-sheet conformation in these solvents. Such gels of beta-sheet peptide based on hierarchical self-assembly consist of nanofiber construction because of the beta-sheet structure, and because of crosslinking attributable to hydrogen bonding among hydroxy groups of the serine side chain.