Unknown

Dataset Information

0

Polymer brush-modified magnetic nanoparticles for His-tagged protein purification.

ABSTRACT: Growth of poly(2-hydroxyethyl methacrylate) brushes on magnetic nanoparticles and subsequent brush functionalization with nitrilotriacetate-Ni(2+) yield magnetic beads that selectively capture polyhistidine-tagged (His-tagged) protein directly from cell extracts. Transmission electron microscopy, Fourier transform infrared (FT-IR) spectroscopy, thermogravimetric analysis, and magnetization measurements confirm and quantify the formation of the brushes on magnetic particles, and multilayer protein adsorption to these brushes results in binding capacities (220 mg BSA/g of beads and 245 mg His-tagged ubiquitin/g of beads) that are an order of magnitude greater than those of commercial magnetic beads. Moreover, the functionalized beads selectively capture His-tagged protein within 5 min. The high binding capacity and protein purity along with efficient protein capture in a short incubation time make brush-modified particles attractive for purification of recombinant proteins.

SUBMITTER: Xu F 

PROVIDER: S-EPMC3153590 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Polymer brush-modified magnetic nanoparticles for His-tagged protein purification.

Xu Fei F   Geiger James H JH   Baker Gregory L GL   Bruening Merlin L ML  

Langmuir : the ACS journal of surfaces and colloids 20110221 6

Growth of poly(2-hydroxyethyl methacrylate) brushes on magnetic nanoparticles and subsequent brush functionalization with nitrilotriacetate-Ni(2+) yield magnetic beads that selectively capture polyhistidine-tagged (His-tagged) protein directly from cell extracts. Transmission electron microscopy, Fourier transform infrared (FT-IR) spectroscopy, thermogravimetric analysis, and magnetization measurements confirm and quantify the formation of the brushes on magnetic particles, and multilayer protei  ...[more]

Similar Datasets

Unknown Magnetic One-Step Purification of His-Tagged Protein by Bare Iron Oxide Nanoparticles.
| S-EPMC6648446 | biostudies-literature
Unknown Ni-modified magnetic nanoparticles for affinity purification of His-tagged proteins from the complex matrix of the silkworm fat body.
| S-EPMC7648358 | biostudies-literature
Unknown One-step selective affinity purification and immobilization of His-tagged enzyme by recyclable magnetic nanoparticles.
| S-EPMC8182278 | biostudies-literature
Unknown Highly-efficient purification of native polyhistidine-tagged proteins by multivalent NTA-modified magnetic nanoparticles.
| S-EPMC2529454 | biostudies-literature
Unknown Direct purification and immobilization of his-tagged enzymes using unmodified nickel ferrite NiFe<sub>2</sub>O<sub>4</sub> magnetic nanoparticles.
| S-EPMC10700653 | biostudies-literature
Unknown Translocation of nanoparticles through a polymer brush-modified nanochannel.
| S-EPMC3407119 | biostudies-other
Unknown Synchronized purification and immobilization of his-tagged β-glucosidase via Fe<sub>3</sub>O<sub>4</sub>/PMG core/shell magnetic nanoparticles.
| S-EPMC5278371 | biostudies-literature
Unknown A Simple and Versatile Strategy for Oriented Immobilization of His-Tagged Proteins on Magnetic Nanoparticles.
| S-EPMC10739578 | biostudies-literature
Unknown Synthesis of magnetic nanoparticles with an IDA or TED modified surface for purification and immobilization of poly-histidine tagged proteins.
| S-EPMC9050487 | biostudies-literature
Unknown Purification and characterisation of recombinant His-tagged RgpB gingipain from Porphymonas gingivalis.
| S-EPMC4682895 | biostudies-literature