| Autor: |
Karchilakis G; Dainton Building, Department of Chemistry, The University of Sheffield, Brook Hill, Sheffield, South Yorkshire S3 7HF, U.K., Varlas S; Dainton Building, Department of Chemistry, The University of Sheffield, Brook Hill, Sheffield, South Yorkshire S3 7HF, U.K., Johnson EC; Dainton Building, Department of Chemistry, The University of Sheffield, Brook Hill, Sheffield, South Yorkshire S3 7HF, U.K., Norvilaite O; Dainton Building, Department of Chemistry, The University of Sheffield, Brook Hill, Sheffield, South Yorkshire S3 7HF, U.K., Farmer MAH; Dainton Building, Department of Chemistry, The University of Sheffield, Brook Hill, Sheffield, South Yorkshire S3 7HF, U.K., Sanderson G; GEO Specialty Chemicals, Hythe, Southampton, Hampshire SO45 3ZG, U.K., Leggett GJ; Dainton Building, Department of Chemistry, The University of Sheffield, Brook Hill, Sheffield, South Yorkshire S3 7HF, U.K., Armes SP; Dainton Building, Department of Chemistry, The University of Sheffield, Brook Hill, Sheffield, South Yorkshire S3 7HF, U.K. |
| Abstrakt: |
Compared to lipids, block copolymer vesicles are potentially robust nanocontainers for enzymes owing to their enhanced chemical stability, particularly in challenging environments. Herein we report that cis -diol-functional diblock copolymer vesicles can be chemically adsorbed onto a hydrophilic aldehyde-functional polymer brush via acetal bond formation under mild conditions (pH 5.5, 20 °C). Quartz crystal microbalance studies indicated an adsorbed amount, Γ, of 158 mg m -2 for vesicle adsorption onto such brushes, whereas negligible adsorption (Γ = 0.1 mg m -2 ) was observed for a control experiment conducted using a cis -diol-functionalized brush. Scanning electron microscopy and ellipsometry studies indicated a mean surface coverage of around 30% at the brush surface, which suggests reasonably efficient chemical adsorption. Importantly, such vesicles can be conveniently loaded with a model enzyme (horseradish peroxidase, HRP) using an aqueous polymerization-induced self-assembly formulation. Moreover, the immobilized vesicles remained permeable toward small molecules while retaining their enzyme payload. The enzymatic activity of such HRP-loaded vesicles was demonstrated using a well-established colorimetric assay. In principle, this efficient vesicle-on-brush strategy can be applied to a wide range of enzymes and functional proteins for the design of next-generation immobilized nanoreactors for enzyme-mediated catalysis. |
