Chromatographic purification of histidine-tagged proteins using zirconia particles modified with phosphate groups

Kanoh, Shogo; Shiraki, Kentaro; Wada, Momoyo; Tanaka, Takeshi; Kitamura, Mitsutaka; Kato, Katsuya; Hirano, Atsushi

doi:10.1016/j.chroma.2023.464112

Journal of Chromatography A

2023

DOI: 10.1016/j.chroma.2023.464112

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Chromatographic purification of histidine-tagged proteins using zirconia particles modified with phosphate groups

Shogo Kanoh

Kentaro Shiraki

Momoyo Wada

et al.

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2024

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Cited by 3 publications

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Ultrafast His‐Tagged Protein Purification

Luo,

Pamidi,

Gardner

et al. 2024

Current Protocols

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This article details how to use a vortex fluidic device (VFD) to accelerate protein purification via immobilized metal affinity chromatography (IMAC). Building upon a previous report of VFD‐based purification, we introduce a membrane insert to simplify the purification protocol and the resin recovery step. This new platform can be adapted to different types of IMAC resins and purification membranes. Proteins can be purified directly from clarified lysate, non‐clarified lysate, and even non‐lysed cultures without concerns of system clogging. Strong binding between the Ni2+ and the target protein's His6‐tag effectively captures the target protein on IMAC resins or membranes placed in the VFD. Continuous flow of different solutions through the VFD allows dynamic binding, washing, and elution of the target protein. Furthermore, the system dramatically accelerates protein purification; a typical purification from cell lysate requires approximately 4 min. Herein, we demonstrate the single‐step purification of two His6‐tagged proteins from both clarified and non‐clarified cell lysates without requiring batch binding. © 2024 The Author(s). Current Protocols published by Wiley Periodicals LLC.Basic Protocol 1: Preparation of the resin‐loaded membrane insert and the vortex fluidic device (VFD) setup prior to purificationBasic Protocol 2: Purification of His6‐tagged proteins using the VFDAlternate Protocol: VFD‐mediated His6‐tagged protein purification from non‐clarified lysateSupport Protocol: Preparation of chemically modified glass fiber membrane for VFD‐mediated immobilized metal affinity chromatography purification

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Ultrafast His‐Tagged Protein Purification

Luo,

Pamidi,

Gardner

et al. 2024

Current Protocols

View full text Add to dashboard Cite

show abstract

Construction of a highly efficient adsorbent for one-step purification of recombinant proteins: Functionalized cellulose-based monolith fabricated via phase separation method

Huang,

Chen,

Zhang

et al. 2024

Carbohydrate Polymers

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Citrate coated iron oxide nanoparticles: Synthesis, characterization, and performance in protein adsorption

Portilla,

López,

Escobedo

et al. 2024

AIMSMATES

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<p>Magnetic nanoparticles (MNPs) are extensively utilized in biomedicine as part of controlled drug release systems, hyperthermia, and magnetic resonance imaging. Surface modification of MNPs not only enhances their stability and biocompatibility but also increases affinity with certain molecules, allowing them to be used in protein separation and adsorption processes. This article reports the synthesis and characterization of iron oxide MNPs functionalized with citric acid (IONPs@CA) to evaluate their performance in protein adsorption. The nanoparticles were characterized using various techniques such as transmission electron microscopy (TEM), X-ray diffraction (XRD), dynamic light scattering (DLS), thermogravimetric analysis (TGA), and Fourier-transform infrared spectroscopy (FT-IR). The percentage of lysozyme (Lyz) adsorbed by IONPs@CA was 84.9%, while the IONPs sample only adsorbed 5.9%. In silico evaluation results showed some repulsion bonds obtained in Lyz-IONPs and hydrogen bonds, carbon-hydrogen bonds, and van der Waals interactions in Lyz-IONPs@CA. These results may be novel since no previous research was found specifying this type of interaction between lysozyme and IONPs and/or IONPs@CA. The maximum adsorption efficiency obtained for the coated nanoparticles was 88.3%.</p>

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Chromatographic purification of histidine-tagged proteins using zirconia particles modified with phosphate groups

Cited by 3 publications

References 40 publications

Ultrafast His‐Tagged Protein Purification

Ultrafast His‐Tagged Protein Purification

Construction of a highly efficient adsorbent for one-step purification of recombinant proteins: Functionalized cellulose-based monolith fabricated via phase separation method

Citrate coated iron oxide nanoparticles: Synthesis, characterization, and performance in protein adsorption

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