Issue 24, 2019

Constructing peptide-based artificial hydrolases with customized selectivity

Abstract

Peptide-based materials are promising building blocks for the fabrication of artificial enzymes due to their proteic nature and tailorable structure. However, it is still a big challenge to create artificial enzymes with designable selectivity. In this study, the molecular imprinting strategy was combined with the self-assembly of Fmoc-FFH to create an artificial hydrolase with specific selectivity. By using p-NPA as the imprinting template, we found that the imprinted polymer that was coated on the surface of the catalytic peptide nanofibers provided a specific binding site to p-NPA, hence enhancing the catalytic efficiency of the artificial hydrolase. Furthermore, we confirmed that the substrate selectivity of this artificial enzyme can be customized by changing the imprinting template. The obtained catalyst is recyclable and exhibits a higher catalytic activity at a wider reaction temperature and pH due to the introduction of the polymer. This study provides a new approach to constructing enzyme mimics with customized substrate selectivity based on the peptide-based material platform.

Graphical abstract: Constructing peptide-based artificial hydrolases with customized selectivity

Supplementary files

Article information

Article type
Paper
Submitted
28 Ақп. 2019
Accepted
30 Сәу. 2019
First published
08 Мам. 2019

J. Mater. Chem. B, 2019,7, 3804-3810

Constructing peptide-based artificial hydrolases with customized selectivity

M. Zhu, M. Wang, W. Qi, R. Su and Z. He, J. Mater. Chem. B, 2019, 7, 3804 DOI: 10.1039/C9TB00408D

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements