Protein purification via consecutive histidine-polyphosphate interaction.
Ni‐NTA
histidine repeats
polyphosphate
protein purification
resin
Journal
Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750
Informations de publication
Date de publication:
Jun 2024
Jun 2024
Historique:
revised:
26
04
2024
received:
17
02
2024
accepted:
29
04
2024
medline:
15
5
2024
pubmed:
15
5
2024
entrez:
15
5
2024
Statut:
ppublish
Résumé
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.
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e5021Subventions
Organisme : New Frontiers in Research Fund
ID : NFRFE-2021-00510
Organisme : Cystic Fibrosis Canada
ID : 1011927
Organisme : Science and Technology Department of Hunan Province
ID : 2022RC4029
Organisme : Science Fund for Distinguished Young Scholars of Hunan Province
ID : 2023JJ10083
Informations de copyright
© 2024 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.
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