Architectural Change of the Shell-Forming Block from Linear to V-Shaped Accelerates Micellar Disassembly, but Slows the Complete Enzymatic Degradation of the Amphiphiles
| Autor: | Lihi Ozery, Tamara Ehm, Merav Segal, Roey J. Amir, Shreyas Shankar Wagle, Gadi Slor, Roy Beck |
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| Jazyk: | angličtina |
| Předmět: |
Polymers and Plastics
Molecular mass Chemistry Polymers Bioengineering 02 engineering and technology 010402 general chemistry 021001 nanoscience & nanotechnology Cleavage (embryo) 01 natural sciences Micelle 0104 chemical sciences Polyethylene Glycols Biomaterials Drug Delivery Systems Chemical engineering Block (programming) Amphiphile Drug delivery PEG ratio Materials Chemistry Nanocarriers 0210 nano-technology Hydrophobic and Hydrophilic Interactions Micelles |
| Zdroj: | Biomacromolecules |
| ISSN: | 1526-4602 1525-7797 |
| DOI: | 10.1021/acs.biomac.0c00882 |
| Popis: | Tuning the enzymatic degradation and disassembly rates of polymeric amphiphiles and their assemblies is crucial for designing enzyme-responsive nanocarriers for controlled drug delivery applications. The common methods to control the enzymatic degradation of amphiphilic polymers are to tune the molecular weights and ratios of the hydrophilic and hydrophobic blocks. In addition to these approaches, the architecture of the hydrophilic block can also serve as a tool to tune enzymatic degradation and disassembly. To gain a deeper understanding of the effect of the molecular architecture of the hydrophilic block, we prepared two types of well-defined PEG-dendron amphiphiles bearing linear or V-shaped PEG chains as the hydrophilic blocks. The high molecular precision of these amphiphiles, which emerges from the utilization of dendrons as the hydrophobic blocks, allowed us to study the self-assembly and enzymatic degradation and disassembly of the two types of amphiphiles with high resolution. Interestingly, the micelles of the V-shaped amphiphiles were significantly smaller and disassembled faster than those of the amphiphiles based on linear PEG. However, the complete enzymatic cleavage of the hydrophobic end groups was significantly slower for the V-shaped amphiphiles. Our results show that the V-shaped architecture can stabilize the unimer state and, hence, plays a double role in the enzymatic degradation and the induced disassembly and how it can be utilized to control the release of encapsulated or bound molecular cargo. |
| Databáze: | OpenAIRE |
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