ArticleChemical science2019
Tunable enzyme responses in amphiphilic nanoassemblies through alterations in the unimer-aggregate equilibrium.
Article in Chemical science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Unimer Exchange as a Tool for Programming Enzymatic Degradation through Micellar Dynamics.Biomacromolecules · 2025Article
- Structural Determinants of Stimuli-Responsiveness in Amphiphilic Macromolecular Nano-assemblies.Progress in polymer science · 2024Article
- Architecture-Based Programming of Polymeric Micelles to Undergo Sequential Mesophase Transitions.ACS macro letters · 2023Article
- Stimuli-Induced Architectural Transition as a Tool for Controlling the Enzymatic Degradability of Polymeric Micelles.ACS polymers Au · 2022Article
- PLLA Coating of Active Implants for Dual Drug Release.Molecules (Basel, Switzerland) · 2022Article
- Multichannel dual protein sensing using amphiphilic supramolecular assemblies.Chemical communications (Cambridge, England) · 2021Article
- Article
- Using High Molecular Precision to Study Enzymatically Induced Disassembly of Polymeric Nanocarriers: Direct Enzymatic Activation or Equilibrium-Based Degradation?Macromolecules · 2021Review
- Disassembly of polymeric nanoparticles with enzyme-triggered polymer unzipping: polyelectrolyte complexes vs. amphiphilic nanoassemblies.Chemical communications (Cambridge, England) · 2020Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
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