A new class of simple, linear, amphiphilic peptides are developed that have the ability to undergo triggered self-assembly into self-supporting hydrogels. Under non-gelling aqueous conditions, these peptides exist in a random coil conformation and peptide solutions have the viscosity of water. On the addition of a buffered saline solution, the peptides assemble into a β-sheet rich network of fibrils, ultimately leading to hydrogelation. A family of nine peptides is prepared to study the influence of peptide length and amino acid composition on the rate of self-assembly and hydrogel material properties. The amino acid composition is modulated by varying residue hydrophobicity and hydrophilicity on the two opposing faces of the amphiphile. The conformation of peptides in their soluble and gel state is studied by circular dichroism (CD), while the resultant material properties of their gels is investigated using oscillatory sheer rheology. One weight percent gels formed under physiological conditions have storage modulus (G′) values that vary from ≈20 to ≈800 Pa, with sequence length and hydrophobic character playing a dominant roll in defining hydrogel rigidity. Based on the structural and functional data provided by the nine-peptide family members, an optimal sequence, namely LK13, is evolved. LK13 (LKLKLKLKLKLKL-NH2) undergoes triggered self-assembly, affording the most rigid gel of those studied (G′=797 ± 105). It displays shear thin-recovery behavior, allowing its delivery by syringe and is cytocompatibile as assessed with murine C3H10t1/2 mesenchymal stem cells.