Fabrication of Polyion Complex Vesicles with Enhanced Salt and Temperature Resistance and Their Potential Applications as Enzymatic Nanoreactors
Integrating catalytic functions into polymeric vesicles through enzyme entrapment is appealing for bioreactor fabrication, yet there are critical issues regarding the regulation of solute transport through membranes and enzyme loading without denaturation. Polyion complex vesicles (PICsomes) with se...
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Published in | Biomacromolecules Vol. 15; no. 7; pp. 2389 - 2397 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Chemical Society
14.07.2014
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Subjects | |
Online Access | Get full text |
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Summary: | Integrating catalytic functions into polymeric vesicles through enzyme entrapment is appealing for bioreactor fabrication, yet there are critical issues regarding the regulation of solute transport through membranes and enzyme loading without denaturation. Polyion complex vesicles (PICsomes) with semipermeable membranes and the propensity to form in water can overcome these issues; however, cross-linking is required for sufficient physiological stability. Herein, we report the first successful fabrication of non-cross-linked PICsomes with sufficient stability at physiological salinity and temperature by tuning the hydrophobicity of the aliphatic side chains in the pendant group of the constituent polyelectrolytes. Dynamic light scattering and transmission electron microscopy revealed that the intervesicular fusion and disintegration of the PICsomes was prevented and a narrow distribution was maintained at physiological salinity and temperatures. Furthermore, their application as enzymatic nanoreactors was verified even in the presence of proteases. As such, the potential utility of the PICsomes in biomedical fields was established. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 |
ISSN: | 1525-7797 1526-4602 |
DOI: | 10.1021/bm500127g |