Campus Units

Chemistry

Document Type

Article

Publication Version

Accepted Manuscript

Publication Date

8-2017

Journal or Book Title

Helvetica Chimica Acta

Volume

100

Issue

8

First Page

e1700147

DOI

10.1002/hlca.201700147

Abstract

Enzymes have substrate‐tailored active sites with optimized molecular recognition and catalytic features. Although many different platforms have been used by chemists to construct enzyme mimics, it is challenging to tune the structure of their active sites systematically. By molecularly imprinting template molecules within doubly cross‐linked micelles, we created protein‐sized nanoparticles with catalytically functionalized binding sites. These enzyme mimics accelerated the hydrolysis of activated esters thousands of times over the background reaction, whereas the analogous catalytic group (a nucleophilic pyridyl derivative) was completely inactive in bulk solution under the same conditions. The template molecules directly controlled the size and shape of the active site and modulated the resulting catalyst's performance at different pHs. The synthetic catalysts displayed Michaelis–Menten enzymatic behavior and, interestingly, reversed the intrinsic reactivity of the activated esters during the hydrolysis.

Comments

This is the peer-reviewed version of the following article: Hu, Lan, and Yan Zhao. "Cross‐Linked Micelles with Enzyme‐Like Active Sites for Biomimetic Hydrolysis of Activated Esters." Helvetica Chimica Acta 100, no. 8 (2017): e1700147., which has been published in final form at DOI: 10.1002/hlca.201700147. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.

Copyright Owner

Wiley-VHCA AG, Zurich, Switzerland

Language

en

File Format

application/pdf

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