Gels prepared with the solvent-triggering method are attractive for their easy and fast preparation; however, the role of solvents in this process remains unclear, which hinders the efficient and accurate control of desired gel properties. In this study, the role of solvents in the solvent-triggering gelation process is studied using 9-fluorenylmethoxycarbonyl (Fmoc)-protected diphenylalanine (Fmoc-FF) as the gelator. Density functional theory (DFT)-based calculations and corresponding wavefunction analyses are conducted to identify the H-bonding interaction sites between the molecules. The calculation results clearly annotate the activating role of DMF and the triggering role of H2O in the gelation process. The solvation of Fmoc-FF by DMF can activate the H-bonding sites on the peptide chain, showing a conformation reversal and higher electrostatic potentials. Then, the H-bonding between Fmoc-FF and H2O is facilitated to trigger gelation. The physical Fmoc-FF/DMF/H2O gels show easily tuned mechanical strengths (G' of 102-105 Pa), injectable potentials (general yield strain < 100%), and stable recoverability (80-98% within 100 s). The regulation of these properties depends on not only the gelator concentration but also the H-bonding interactions with solvent molecules, which have seldom been studied in detail before. By understanding the effect of solvents, low-molecular-weight gelator-based gels can be designed, prepared, and tuned efficiently for potential applications.