Self-assembling peptide hydrogels create finely tunable microenvironments to promote cell proliferation and differentiation . Previous work has shown that such hydrogels can be chemically modified while retaining physical characteristics and are capable of protecting cells during syringe injection. Racemic mixtures of peptide hydrogels add another dimension of tunability to alter hydrogel stiffness and chemical cues in the environment. Here, we study racemic hydrogels of the Rapidly Assembling Pentapeptides for Injectable Delivery (RAPID) KYFIL sequence to determine gel stiffness and chemical characteristics as well as viability with cell culture. L- and D-form KYFIL have similar storage moduli and stress-recovery times, while the 50:50 racemic mixture was found to have a storage modulus that was 66% of the L-form and take up to 2.3x longer than the L-form to recover after being strained. FTIR indicated that L- and D-form KYFIL assembled in antiparallel beta sheet complexes, while the 50:50 racemic mixture formed in parallel beta sheets. As found rheology results were in contrast with other published works, we recreated a similar known hydrogel. Rheology of this sequence indicated that the racemic mixture was stiffer than either the L- or D-form, confirming previously published results. Our interesting and unexpected findings indicate that the KYFIL peptide sequence has assembly mechanisms in racemic mixtures unique to previously studied sequences, revealing novel hydrogel formations.