Preorganization boosts the artificial esterase activity of a self-assembling peptide

The creation of artificial enzymes to mimic natural enzymes remains a great challenge owing to the complexity of the structural arrangement of the essential amino acids in catalytic centers. In this study, we used the phosphatase-based enzyme-instructed self-assembly (EISA) to supervise artificial e...

Full description

Saved in:
Bibliographic Details
Published in:Science China. Chemistry 2021-09, Vol.64 (9), p.1554-1559
Main Authors: Chen, Yaoxia, Zhang, Wenwen, Ding, Yinghao, Liang, Chunhui, Shi, Yang, Hu, Zhi-Wen, Wang, Ling, Yang, Zhimou
Format: Article
Language:English
Subjects:
Alkaline phosphatase
Amino acids
Biology
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Enzyme kinetics
Enzymes
Esterases
Peptides
Phosphatase
Phosphorylation
Precursors
Self-assembly
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The creation of artificial enzymes to mimic natural enzymes remains a great challenge owing to the complexity of the structural arrangement of the essential amino acids in catalytic centers. In this study, we used the phosphatase-based enzyme-instructed self-assembly (EISA) to supervise artificial esterases’ final structures and catalytic activities. We reported that peptide precursors containing different phosphorylation sites could preorganize into alternated nanostructures and undergo dephosphorylation in the presence of alkaline phosphatase (ALP) with variation in kinetic and thermodynamic profiles. Although identical self-assembly compositions were formed after dephosphorylation, precursors with more enhanced preorganized states tended to better promote ALP dephosphorylation, facilitate further self-assembly, and strengthen the catalytic activities of the final assemblies. We envisioned that our strategy would be useful for further construction and manipulation of various artificial enzymes with superior catalytic activities.
ISSN:1674-7291
1869-1870
DOI:10.1007/s11426-021-1029-x