A new Schiff base, 2 hydroxy 1 napthaldehyde 2 amino thiazole(HNATS) and its Cu(Ⅱ) complex was synthesized. The complex[Cu(Ⅱ) (HNATS) 2] could exhibit an efficient peroxitase like catalytic activity, and catalyze th...A new Schiff base, 2 hydroxy 1 napthaldehyde 2 amino thiazole(HNATS) and its Cu(Ⅱ) complex was synthesized. The complex[Cu(Ⅱ) (HNATS) 2] could exhibit an efficient peroxitase like catalytic activity, and catalyze the coupling reaction of 2,4 dichlorophenol and 4 amino antipyrine with hydrogen peroxide. The effect of SDS on the catalytic activity of mimetic enzyme was studied. Based on the reaction, the determination of O ·- 2 by this new spectrophotometric method was developed. The proposed method was used to determine SOD activity of garlic, scallion and onion with satisfactory results.展开更多
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/disa...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 Nap FFEYIH(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 Nap FFEYp IH(Yp H) 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 Yp H 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.展开更多
文摘A new Schiff base, 2 hydroxy 1 napthaldehyde 2 amino thiazole(HNATS) and its Cu(Ⅱ) complex was synthesized. The complex[Cu(Ⅱ) (HNATS) 2] could exhibit an efficient peroxitase like catalytic activity, and catalyze the coupling reaction of 2,4 dichlorophenol and 4 amino antipyrine with hydrogen peroxide. The effect of SDS on the catalytic activity of mimetic enzyme was studied. Based on the reaction, the determination of O ·- 2 by this new spectrophotometric method was developed. The proposed method was used to determine SOD activity of garlic, scallion and onion with satisfactory results.
基金supported by the National Natural Science Foundation of China (22234002,22204019,82172097)the Postgraduate Research&Practice Innovation Program of Jiangsu Province(KYCX22_0245)。
文摘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 Nap FFEYIH(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 Nap FFEYp IH(Yp H) 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 Yp H 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.
