Journal
MACROMOLECULAR RAPID COMMUNICATIONS
Volume 41, Issue 18, Pages -Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/marc.202000208
Keywords
enzymes; Forster resonance energy transfer; polyion complex micelles; protein delivery
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Funding
- Australian Research Council (ARC) [DE170100315, DP170101191]
- Australian Research Council [DE170100315] Funding Source: Australian Research Council
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Although a range of polymer-protein polyion complex (PIC) micelle systems have been developed in the literature, relatively little attention has been paid to the influence of polymer structure on the assembly, or to the mechanism of disassembly. In this work, Forster resonance energy transfer is used in combination with light sheet fluorescence microscopy and isothermal calorimetry to monitor the formation and stability of PIC micelles with various carboxylic-acid-based binding blocks in MCF-7 cancer spheroid models. All micelles are stable in the presence of free protein, but are unstable in solutions with an ionic strength >200 mmand prone to disassembly at reduced pH. Introducing carbon spacers between the backbone and the binding carboxylic acid results in improved PIC micelle stability at physiological pH, but also increases the pK(a)of the binding moiety, resulting in improved protein release upon cell uptake. These results give important insights into how to tune PIC micelle stability for controlled protein release in biological environments.
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