Taking Advantage of Hydrophobic Fluorine Interactions for Self-Assembled Quantum Dots as a Delivery Platform for Enzymes
Autor: | Mónica Carril, Mona Atabakhshi-Kashi, Khosro Khajeh, Wolfgang J. Parak, Carolina Carrillo-Carrión |
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Rok vydání: | 2018 |
Předmět: |
Surface Properties
Kinetics Nanoparticle Nanotechnology 02 engineering and technology 010402 general chemistry 01 natural sciences Catalysis Hydrophobic effect Colloid Quantum Dots Particle Size Laccase 010405 organic chemistry Chemistry Fluorine General Medicine General Chemistry Hydrogen-Ion Concentration 021001 nanoscience & nanotechnology 0104 chemical sciences Quantum dot alpha-Galactosidase Self-assembly 0210 nano-technology Hydrophobic and Hydrophilic Interactions |
Zdroj: | Angewandte Chemie International Edition. 57:5033-5036 |
ISSN: | 1433-7851 |
DOI: | 10.1002/anie.201801155 |
Popis: | Self-assembly of nanoparticles provides unique opportunities as nanoplatforms for controlled delivery. By exploiting the important role of noncovalent hydrophobic interactions in the engineering of stable assemblies, nanoassemblies were formed by the self-assembly of fluorinated quantum dots in aqueous medium through fluorine-fluorine interactions. These nanoassemblies encapsulated different enzymes (laccase and α-galactosidase) with encapsulation efficiencies of ≥74 %. Importantly, the encapsulated enzymes maintained their catalytic activity, following Michaelis-Menten kinetics. Under an acidic environment the nanoassemblies were slowly disassembled, thus allowing the release of encapsulated enzymes. The effective release of the assayed enzymes demonstrated the feasibility of this nanoplatform to be used in pH-mediated enzyme delivery. In addition, the as-synthesized nanoassemblies, having a diameter of about 50 nm, presented high colloidal stability and fluorescence emission, which make them a promising multifunctional nanoplatform. |
Databáze: | OpenAIRE |
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