Nickel hydroxide/hydroxyapatite nanorods as affinity adsorbents for separation histidine-tagged proteins. (April 2015)

• Record Type: Journal Article
• Authors: Yao, Shasha; Li, Guofang; Li, Binjie; Zhao, Yanbao; Sun, Lei; Qu, Peng
• Is Part Of: Materials research bulletin. Volume 64(2015:Apr.)
• Page Start: 200
• Page End: 206
• Publication Date: 2015-04
• Subjects: A. Composites -- B. Chemical synthesis -- C. Thermogravimetric analysis -- C. Transmission electron microscopy; Materials -- Periodicals; Crystal growth -- Periodicals; Matériaux -- Périodiques; Cristaux -- Croissance -- Périodiques; Crystal growth; Materials; Periodicals; 620.11
• DOI: 10.1016/j.materresbull.2014.12.070
• Languages: English
• ISSNs: 0025-5408

Abstract

Graphical abstract: Highlights: Ni(OH)2 /HAP nanorods are synthesized by hydrothermal method. Their morphology depends strongly on the reaction condition. Ni(OH)2 /HAP nanorods can be used to separate His-tagged proteins. Ni(OH)2 /HAP nanorods present high protein binding ability. Abstract: Nickel hydroxide/hydroxyapatite (designated as Ni(OH)2 /HAP) nanorods have been designed and synthesized by hydrothermal method. The size and morphology of Ni(OH)2 /HAP sample depend strongly on the reaction condition, and introduction of small amount of Ni 2+ ions would be propitious to get the smaller size nanorods. By taking advantage of the high affinity of Ni 2+ ions toward histidine-tagged (His-tagged) proteins, the Ni(OH)2 /HAP nanorods can be used to enrich and separate His-tagged proteins directly from a mixture of lysed cells, and their universality was evaluated by separating three kinds of His-tagged proteins. The Ni(OH)2 /HAP nanorods present negligible nonspecific protein adsorption and high protein binding ability, and their specificity and affinity toward His-tagged proteins can be remained after 4 times recycling. The Ni(OH)2 /HAP nanorods may provide many potential applications for the detection or separation of different biomolecules.