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

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.