Issue 10, 2019

Tunable enzyme responses in amphiphilic nanoassemblies through alterations in the unimer–aggregate equilibrium

Abstract

Developing design rules that offer tailorability in materials' response to enzymes is of great importance, as such materials are of interest in a variety of biomedical applications including sensing, diagnostics and drug delivery. Using an amphiphilic oligomeric platform, we show that the degree of polymerization and hydrophilic–lipophilic balance variations can be utilized to alter the unimer–aggregate equilibrium, which in turn offers robust tunability of the host–guest properties of the amphiphilic nanoassemblies. We found that oligomeric assemblies with higher degree of polymerization are less sensitive to enzymatic degradation and release the guest molecules at a slower rate. Similarly, increasing the hydrophilicity makes these assemblies more sensitive to enzymes. These trends can be understood by correlating these changes to predictable modifications in the dynamics of the unimer–aggregate equilibrium, which affects the substrate availability for enzymes. These findings provide insights into rationally tuning the response of enzyme-sensitive supramolecular assemblies.

Graphical abstract: Tunable enzyme responses in amphiphilic nanoassemblies through alterations in the unimer–aggregate equilibrium

Supplementary files

Article information

Article type
Edge Article
Submitted
24 Oct 2018
Accepted
11 Jan 2019
First published
15 Jan 2019
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2019,10, 3018-3024

Tunable enzyme responses in amphiphilic nanoassemblies through alterations in the unimer–aggregate equilibrium

J. Gao, H. Wang, J. Zhuang and S. Thayumanavan, Chem. Sci., 2019, 10, 3018 DOI: 10.1039/C8SC04744H

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