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Peptides are a promising class of gelators and specifically, cyclic-di-amino acids (CdAA) have great versatility and biocompatibility due to their amino acid side chain diversity. This allows custom programing of the molecular motifs responsible for self-assembly. Six pairs of di-peptides were tested in 25 solvents, of which 16 combinations resulted in a gel. Each of the amino acids selected have unique properties in self-assembly and the 25 solvents represent a broad spectrum of solvent conditions, allowing the result to be extrapolated to untested solvents. The ability to self-assemble into fibrous structures requires a meticulous balance amongst opposing factors, including solubility and those that control growth into elongated aggregates/fibers. The fibrous inter-woven peptide nanofibers from self-assembled CdAA form enormous aspect ratio fibers. The crystal morphology of the resultant gels drastically varied, which is attributed to changes in the side chains, as well as the thermodynamic driving force, being either slow cooling or electrospinning (rapid solvent evaporation). As shown, phenylalanine and leucine when cyclized at a 2% wt in canola oil formed a fibrillar network. Fiber formation was characterized using atomic force, scanning electron, brightfield and polarized light microscopies, as well as X-ray diffraction. Additionally, the 16 gels were examined for fiber formation using Hansen Solubility parameters.