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Zwitterionic Polyelectrolyte Complex Vesicles Assembled from Homopoly(2-Oxazoline)s as Enzyme Catalytic Nanoreactors for Potent Anti-Tumor Efficiency.
- Source :
-
Langmuir : the ACS journal of surfaces and colloids [Langmuir] 2024 Sep 17; Vol. 40 (37), pp. 19423-19429. Date of Electronic Publication: 2024 Jul 31. - Publication Year :
- 2024
-
Abstract
- Enzymes are known for their remarkable catalytic efficiency across a wide range of applications. Here, we present a novel and convenient nanoreactor platform based on zwitterionic polyelectrolyte complex vesicles (PCVs), assembled from oppositely charged homopoly(2-oxazoline)s, facilitating enzyme immobilization. We show remarkable enhancements in catalytic activity and stability by encapsulation of lipase as a model enzyme. Even as the temperature rises, the performance of the lipase remains robust. Further, the structural characteristics of PCVs, including hollow architecture and semipermeable membranes, endow them with unique advantages for enzyme cascade reactions involving glucose oxidase (GOx) and horseradish peroxidase (HRP). A decline in catalytic efficiency is shown when the enzymes are individually loaded and subsequently mixed, in contrast to the coloaded GOx-HRP-PCV group. We demonstrate that the vesicle structures establish confined environments where precise enzyme-substrate interactions facilitate enhanced catalytic efficiency. In addition, the nanoreactors exhibit excellent biocompatibility and efficient anti-tumor activity, which hold significant promise for biomedical applications within enzyme-based technologies.
- Subjects :
- Humans
Lipase chemistry
Lipase metabolism
Biocatalysis
Oxazoles chemistry
Polyelectrolytes chemistry
Glucose Oxidase chemistry
Glucose Oxidase metabolism
Horseradish Peroxidase chemistry
Horseradish Peroxidase metabolism
Enzymes, Immobilized chemistry
Enzymes, Immobilized metabolism
Antineoplastic Agents chemistry
Antineoplastic Agents pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 1520-5827
- Volume :
- 40
- Issue :
- 37
- Database :
- MEDLINE
- Journal :
- Langmuir : the ACS journal of surfaces and colloids
- Publication Type :
- Academic Journal
- Accession number :
- 39083025
- Full Text :
- https://doi.org/10.1021/acs.langmuir.4c01729