Molecular Hydrogels with Esterase-like Activity

The development of molecular hydrogels that can be applied for mimicking bioactive molecules attracts extensive interests of researchers in fields of self-assembly. In this study, we reported on several molecular hydrogels based on naphthylacetic acid-peptides containing L -histidine formed by the heating-cooling process. All hydrogels exhibited higher activity to hydrolyze 4-nitrophenyl acetate (4-NPA) than the free L -histidine probably due the high density of L -histidine residue at the surface of self-assembled nanofibers. To calculate the 4-NPA hydrolysis rates, the Michaelis-Menten enzyme kinetics model was made. Among these gels, the gel of Nap-GFFYGHY possesses the highest enzyme activity of making the ester bond cleavage, which is approximately 25 times higher than that of the control (free L -histidine and Nap-GFFYGYY). These results indicate that molecular hydrogels with self-assembled nanofibers have great potential for the generation of self-assembled multivalent materials.