Highly-efficient purification of native polyhistidine-tagged proteins by multivalent NTA-modified magnetic nanoparticles.

Highly-efficient purification of native polyhistidine-tagged proteins by multivalent NTA-modified magnetic nanoparticles. Research Abstract Details 

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Highly-efficient purification of native polyhistidine-tagged proteins by multivalent NTA-modified magnetic nanoparticles. Abstract Text:

Jason S Kim,C Alexander Valencia,Rihe Liu,Wenbin Lin,

A new bis-nitrilotriacetic acid (NTA) chelate with catechol anchor was synthesized and immobilized on superparamagnetic iron oxide nanoparticles. When loaded with Ni(II), these bis-NTA-immobilized nanoparticles were shown to bind polyhistidine (His x 6-tagged) fusion proteins in their native, folded conformations that commercial microbeads failed to bind under identical conditions. Control experiments with a mono-NTA chelate immobilized on iron oxide nanoparticles indicate a similarly high affinity for His x 6-tagged native proteins, suggesting that the high density of the mono-NTA chelate presented by the nanoparticles allows the binding of the His x 6-tag to more than one Ni-NTA moiety on the surface. This study shows that the multivalency strategy can be utilized to enhance the binding of His x 6-tagged proteins in their native, folded conformations. We further demonstrated the selective purification of His x 6-tagged proteins from crude cell lysates by using the Ni(II)-loaded iron oxide nanoparticles. The present platform is capable of efficient purification of His x 6-tagged proteins that are expressed at low levels in mammalian cells. This work thus presents a novel nanoparticle-based high-capacity protein purification system with shorter incubation times, proportionally large washes, and significantly smaller elution volumes compared to commercially available microbeads.

Highly-efficient purification of native polyhistidine-tagged proteins by multivalent NTA-modified magnetic nanoparticles. Publishing Authors By Initials

JS Kim,CA Valencia,R Liu,W Lin,

For similar enzymes and coenzymes: enzymes: hydrolases: esterases: thiolester hydrolases: ubiquitin thiolesterase research abstracts see: enzymes and coenzymes: enzymes: hydrolases: esterases: thiolester hydrolases: ubiquitin thiolesterase research

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Highly-efficient purification of native polyhistidine-tagged proteins by multivalent NTA-modified magnetic nanoparticles. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Bioconjugate chemistry

VOLUME: 18

Page Numbers: 333-41

Journal Abbreviation: Bioconjug. Chem.

ISSN: 1043-1802

DAY: 21

MONTH: 02

YEAR: 2007

Highly-efficient purification of native polyhistidine-tagged proteins by multivalent NTA-modified magnetic nanoparticles. Information

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LANGUAGE: eng

NlmUniqueID: 9010319

Highly-efficient purification of native polyhistidine-tagged proteins by multivalent NTA-modified magnetic nanoparticles. Keywords Mesh Terms:

KEYWORDS: Ubiquitin Thiolesterase

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: Highly-efficient purification of native polyhistidine-tagged proteins by multivalent NTA-modified magnetic nanoparticles. Information

Substance Name: Ubiquitin Thiolesterase

Registry Number: EC 3.1.2.15

Grant and Affiliation Information for Highly-efficient purification of native polyhistidine-tagged proteins by multivalent NTA-modified magnetic nanoparticles.

AFFILIATION: Department of Chemistry and School of Pharmacy and Carolina Center for Genome Sciences, University of North Carolina, Chapel Hill, North Carolina 27599, USA.

Country: United States

AGENCY: United States NCI

GRANT: U54-CA119343

ACRONYM: CA

MEDLINETA: Bioconjug Chem

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