morphological versatility in the selfassembly of valala and alaval dipeptides since the discovery of dipeptide selfassembly diphenylalanine phephebased dipeptides have been widely investigated in a variety of fields although various supramolecular phephebased structures including tubes vesicles fibrils sheets necklaces flakes ribbons and wires have been demonstrated by manipulating the external physical or chemical conditions applied studies of the morphological diversity of dipeptides other than phephe are still required to understand both how these small molecules respond to external conditions such as the type of solvent and how the peptide sequence affects selfassembly and the corresponding molecular structures in this work we investigated the selfassembly of valinealanine valala and alaninevaline alaval dipeptides by varying the solvent medium it was observed that valala dipeptide molecules may generate unique selfassemblybased morphologies in response to the solvent medium used interestingly when alaval dipeptides were utilized as a peptide source instead of valala we observed distinct differences in the final dipeptide structures we believe that such manipulation may not only provide us with a better understanding of the fundamentals of the dipeptide selfassembly process but also may enable us to generate novel peptidebased materials for various applications