Jump to main content
Jump to site search


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

Author affiliations

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

Back to tab navigation

Supplementary files

Publication details

The article was received on 19 Dec 2018, accepted on 28 Jan 2019 and first published on 28 Jan 2019


Article type: Communication
DOI: 10.1039/C8NR10258A
Citation: Nanoscale, 2019, Advance Article

  •   Request permissions

    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, Advance Article , DOI: 10.1039/C8NR10258A

Search articles by author

Spotlight

Advertisements