期刊
BIOCONJUGATE CHEMISTRY
卷 18, 期 1, 页码 183-189出版社
AMER CHEMICAL SOC
DOI: 10.1021/bc060215j
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- NIBIB NIH HHS [EB003809] Funding Source: Medline
- NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING [R21EB003809] Funding Source: NIH RePORTER
This paper describes the bioconjugation of histidine-tagged enzymes and other proteins to the surface of composite magnetomicelles consisting of magnetic gamma-Fe2O3 nanoparticles encapsulated within cross-linked polystyrene-block-polyacrylate copolymer micelle shells. Free carboxylic acid groups on the magnetomicelle surface were converted to Cu2+-iminodiacetic acid (IDA) for protein capture. The conjugation of T4 DNA ligase and enhanced green fluorescent protein to magnetomicelles revealed that proteins were captured with a high surface density and could be magnetically separated from reaction mixtures and subsequently released from the nanoparticle surface. Additionally, bioconjugation of T7 RNA polymerase yielded a functional enzyme that maintained its biological activity and could be recycled for up to three subsequent transcription reactions. We propose that protein-magnetomicelle bioconjugates are effective for protein bioseparation and enzymatic recycling and further strengthen the idea that nanoparticle surfaces have utility in protein immobilization.
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