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The selfassembly of peptides is a key direction for fabrication of advanced materials. Novel approaches for fine tuning of macroscopic and microscopic properties of peptide selfassemblies are of a high demand for constructing biomaterials with desired properties. In this work, while studying the kinetics of the FmocDiphenylalanine (FmocFF) dipeptide selfassembly using the Thioflavin T (ThT) dye, we observed that the presence of ThT strongly modifies structural and mechanical properties of the FmocFF hydrogel. Notably, the presence of ThT resulted in a tenfold increase of the gelation time and in the formation of short and dense fibers in the hydrogel. As a result of these morphological alteration higher thermal stability, and most important, tenfold increase of the hydrogel rigidity was achieved. Hence, ThT not only slowed the kinetics of the FmocFF hydrogel formation, but also strongly enhanced its …