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Issue 8, 2019
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A remote optically controlled hydrolase model based on supramolecular assembly and disassembly of its enzyme-like active site

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Abstract

A photoresponsive hydrolase model was constructed through the spatial organization of histidine/arginine-containing peptide supra-amphiphiles that are held together by cucurbit[8]uril (CB[8]) methylviologen (MV) azobenzene (Azo) ternary complexation and subsequently self-assemble into highly uniform giant vesicles. The reversible morphological transition of the vesicular structures to non-assembled peptide fragments was triggered by azobenzene photoisomerization. This enables the assembly/disassembly of its enzyme-like active site to cause a dramatic change in hydrolytic activity. The dynamic process can be directly monitored to determine the supramolecular structure-related enzymatic parameters, which may help to understand how the regulation of enzyme activity is coupled to the aggregation behaviors of natural enzymes.

Graphical abstract: A remote optically controlled hydrolase model based on supramolecular assembly and disassembly of its enzyme-like active site

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Article information


Submitted
19 Dec 2018
Accepted
28 Jan 2019
First published
28 Jan 2019

Nanoscale, 2019,11, 3521-3526
Article type
Communication

A remote optically controlled hydrolase model based on supramolecular assembly and disassembly of its enzyme-like active site

N. Ma, F. Li, S. Li, S. Chu, L. Han, S. Liu, T. Yan, R. Tian, Q. Luo and J. Liu, Nanoscale, 2019, 11, 3521
DOI: 10.1039/C8NR10258A

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