부산대학교 도서관

Mimetic enzymes are devised as alternates or supplements of natural enzymes in broad fields but regulating their activities in a switchable manner remains challenging. Herein, we proposed an enzymatic self-assembly/disassembly strategy to address this issue. A peptide molecule NapFFEYIH (YH) was rationally designed which, after self-assembling into nanofibers, lined up the histidine moieties to form active hydrolysis centers for mimicking hydrolase activity. Enzymatic dephosphorylation of NapF-FEYpIH (YpH) by alkaline phosphatase to yield YH also turned “ON” the hydrolase activity. In turn, phosphorylation of YH by phosphokinase epidermal growth factor receptor to yield YpH disassembled the nanofibers and thus turned the activity “OFF”. As such, the “ON”/“OFF” of the mimetic hydrolase activities could be regulated under physiological conditions through ALP/EGFR-mediated self-assembly/disassembly of histidine nanofibers. This work provides a feasible strategy for the on-demand fabrication of artificial enzymes with controllable and superior activities.