Influence of self-assembling nonsubstrates on the enzymatic postmodification of peptide supramolecules

Abstract The enzymatic postmodification of supramolecules with functional motifs is a promising approach for preparing tailor-made bioactive materials. We attempted to improve the enzyme reactivity of the previously developed, self-assembling aromatic peptide amphiphile, Fmoc-L3QG, by incorporating other self-assembling components, Fmoc-Ln (n = 2, 3), without the enzyme recognition moiety. Although microscopic and spectroscopic studies suggested neither the nonsubstrate peptide amphiphile coassembled with Fmoc-L3QG, the presence of the short fibril–forming Fmoc-L2 and long fibril–forming Fmoc-L3 increased and decreased, respectively, the enzymatic reactivity of Fmoc-L3QG. The findings here suggest that the supramolecular morphologies play a role in modulating the enzyme reaction environment.