ArticleProtein science : a publication of the Protein Society2024
Protein purification via consecutive histidine-polyphosphate interaction.
Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- The optimization of thermostable recombinant α-amylase for efficient fabric desizing using response surface methodology and surface morphology analysis.Bioprocess and biosystems engineering · 2026Article
- Polyphosphate as a novel regulator of super-enhancer complexes: disruption of phase separation and gene expression.Nucleic acids research · 2026Article
- C-terminal Poly-histidine Tags Alter Escherichia coli Polyphosphate Kinase Activity and Susceptibility to Inhibition.Journal of molecular biology · 2024Article
- Protein purification via consecutive histidine-polyphosphate interaction.Protein science : a publication of the Protein Society · 2024Article
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Authors and funding
4 authors.
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Abstract
While nickel-nitrilotriacetic acid (Ni-NTA) has greatly advanced recombinant protein purification, its limitations, including nonspecific binding and partial purification for certain proteins, highlight the necessity for additional purification such as size exclusion and ion exchange chromatography. However, specialized equipment such as FPLC is typically needed but not often available in many laboratories. Here, we show a novel method utilizing polyphosphate (polyP) for purifying proteins with histidine repeats via non-covalent interactions. Our study demonstrates that immobilized polyP efficiently binds to histidine-tagged proteins across a pH range of 5.5-7.5, maintaining binding efficacy even in the presence of reducing agent DTT and chelating agent EDTA. We carried out experiments of purifying various proteins from cell lysates and fractions post-Ni-NTA. Our results demonstrate that polyP resin is capable of further purification post-Ni-NTA without the need for specialized equipment and without compromising protein activity. This cost-effective and convenient method offers a viable approach as a complementary approach to Ni-NTA.
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Registered trials
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