NiCoMnO4: A Bifunctional Affinity Probe for His-Tagged Protein Purification and Phosphorylation Sites Recognition

Xiaoyue Qi; Long Chen; Chaoqun Zhang; Xinyuan Xu; Yiding Zhang; Yu Bai; Huwei Liu

doi:10.1021/acsami.6b04280

NiCoMnO₄: A Bifunctional Affinity Probe for His-Tagged Protein Purification and Phosphorylation Sites Recognition

Xiaoyue Qi, Long Chen, Chaoqun Zhang, Xinyuan Xu, Yiding Zhang, Yu Bai^*, Huwei Liu

^*Corresponding author for this work

Peking University

Research output: Contribution to journal › Article › peer-review

23 Citations (Scopus)

Abstract

A bifunctional affinity probe NiCoMnO₄ was designed and prepared with controllable morphology and size using facile methods. It was observed that the probe could be applied in His-tagged proteins purification and phosphopeptides enrichment simply through the buffer modulation. NiCoMnO₄ particles showed satisfactory cycling performance for His-tagged proteins purification and broad pH-tolerance of loading buffer for phosphopeptides affinity. Therefore, a high-throughput, cost-effective, and efficient protein/peptide purification method was developed within 10 min based on the novel bifunctional affinity probe.

Original language	English
Pages (from-to)	18675-18683
Number of pages	9
Journal	ACS applied materials & interfaces
Volume	8
Issue number	29
DOIs	https://doi.org/10.1021/acsami.6b04280
Publication status	Published - 27 Jul 2016
Externally published	Yes

Keywords

His-tagged proteins purification
affinity probes
buffer modulation
metal oxide
phosphopeptides enrichment

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10.1021/acsami.6b04280

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abstract = "A bifunctional affinity probe NiCoMnO4 was designed and prepared with controllable morphology and size using facile methods. It was observed that the probe could be applied in His-tagged proteins purification and phosphopeptides enrichment simply through the buffer modulation. NiCoMnO4 particles showed satisfactory cycling performance for His-tagged proteins purification and broad pH-tolerance of loading buffer for phosphopeptides affinity. Therefore, a high-throughput, cost-effective, and efficient protein/peptide purification method was developed within 10 min based on the novel bifunctional affinity probe.",

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author = "Xiaoyue Qi and Long Chen and Chaoqun Zhang and Xinyuan Xu and Yiding Zhang and Yu Bai and Huwei Liu",

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T2 - A Bifunctional Affinity Probe for His-Tagged Protein Purification and Phosphorylation Sites Recognition

AU - Qi, Xiaoyue

AU - Chen, Long

AU - Zhang, Chaoqun

AU - Xu, Xinyuan

AU - Zhang, Yiding

AU - Bai, Yu

AU - Liu, Huwei

PY - 2016/7/27

Y1 - 2016/7/27

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AB - A bifunctional affinity probe NiCoMnO4 was designed and prepared with controllable morphology and size using facile methods. It was observed that the probe could be applied in His-tagged proteins purification and phosphopeptides enrichment simply through the buffer modulation. NiCoMnO4 particles showed satisfactory cycling performance for His-tagged proteins purification and broad pH-tolerance of loading buffer for phosphopeptides affinity. Therefore, a high-throughput, cost-effective, and efficient protein/peptide purification method was developed within 10 min based on the novel bifunctional affinity probe.

KW - His-tagged proteins purification

KW - affinity probes

KW - buffer modulation

KW - metal oxide

KW - phosphopeptides enrichment

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ER -

NiCoMnO₄: A Bifunctional Affinity Probe for His-Tagged Protein Purification and Phosphorylation Sites Recognition

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Keywords

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