Ni(II)-decorated porous titania microspheres as a stationary phase for column chromatography applications: Highly selective purification of hemoglobin from human blood

Kip, Çiğdem; Tosun, Rukiye Babacan; Alpaslan, Sezgi; Koçer, İlkay; Çelik, Eda; Tuncel, Alï

doi:10.1016/j.talanta.2019.03.045

Cited by 32 publications

(12 citation statements)

References 34 publications

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“…Likewise, Cu (II), Ni (II), Co (II), and Zn (II) cations are also used to purify proteins containing histidine residues [47][48][49][50]. High selectivity is achieved by the interaction of the immobilized cation with the imidazole ring of the histidine residues in peptides and proteins [47][48][49][50]. IMAC was first proposed by Porath et al using an affinity sorbent, which was prepared by the immobilization of metal cation (Ni(II) and Cu(II)) on agarose using IDA as a chelating ligand, for the purification of histidine-containing proteins [51].…”

Section: Immobilized Metal Affinity Chromatographymentioning

confidence: 99%

“…Likewise, Cu (II), Ni (II), Co (II), and Zn (II) cations are also used to purify proteins containing histidine residues [47–50]. High selectivity is achieved by the interaction of the immobilized cation with the imidazole ring of the histidine residues in peptides and proteins [47–50]. IMAC was first proposed by Porath et al.…”

Section: Bioaffinity Chromatography Techniquesmentioning

confidence: 99%

“…Highly selective purification of hemoglobin from human blood was performed using Ni(II)‐decorated, monodisperse‐porous titania microspheres as a stationary phase in a fused silica capillary tubing [48]. Highly selective magnetic affinity purification of histidine‐tagged (His‐tagged) proteins was performed using Ni(II) attached‐iminodiacetic acid functionalized‐magnetic, uniform‐porous silica microspheres in batch fashion [65].…”

Section: Bioaffinity Chromatography Techniquesmentioning

confidence: 99%

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Recent trends in sorbents for bioaffinity chromatography

Kip

Hamaloğlu

Demir

et al. 2021

J of Separation Science

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Isolation or enrichment of biological molecules from complex biological samples is mostly a prerequisite in proteomics, genomics, and glycomics. Different techniques have been used to advance the efficiency of the purification of biological molecules. Bioaffinity chromatography is one of the most powerful technique that plays an important role in the isolation of target biological molecules by the specific interactions with ligands that are immobilized on different support materials. This review examines the recent developments in bioaffinity chromatography particularly over the past 5 years in the literature. Also properties of supports, immobilization techniques, types of binding agents, and methods used in bioaffinity chromatography applications are summarized.

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Section: Immobilized Metal Affinity Chromatographymentioning

confidence: 99%

Section: Bioaffinity Chromatography Techniquesmentioning

confidence: 99%

Section: Bioaffinity Chromatography Techniquesmentioning

confidence: 99%

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Recent trends in sorbents for bioaffinity chromatography

Kip

Hamaloğlu

Demir

et al. 2021

J of Separation Science

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“…[19][20][21] Further research on MOAC has led to metal oxides being modified on various substrates, such as diatomite, magnetic Fe 3 O 4 , 22 and graphene (G), to enrich phosphopeptides. 23 Among these substrates, carbon-based materials have become a significant group due to their good physical and chemical properties.…”

Section: Introductionmentioning

confidence: 99%

“…Various metal oxides, such as lanthanum oxide, 19 zirconium oxide, 20 and titania, 21 have been developed and widely used for the effective enrichment of phosphopeptides 19–21 . Further research on MOAC has led to metal oxides being modified on various substrates, such as diatomite, magnetic Fe 3 O 4 , 22 and graphene (G), to enrich phosphopeptides 23 . Among these substrates, carbon‐based materials have become a significant group due to their good physical and chemical properties.…”

Section: Introductionmentioning

confidence: 99%

In situ synthesis of a novel metal oxide affinity chromatography affinity probe for the selective enrichment of low‐abundance phosphopeptides

Wang

Yan

et al. 2020

Rapid Comm Mass Spectrometry

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Rationale Due to the dynamic nature of phosphorylation states and the low stoichiometry of phosphopeptides, it is still a challenge to efficiently capture phosphopeptides from complex biological samples before mass spectrometry analysis. Among the enrichment strategies, metal oxide affinity chromatography (MOAC) is one of the most widely used and the one with the most potential. It is based on reversible Lewis acid–base interactions between the metal oxides and the negatively charged phosphate groups to achieve the specific selection of phosphopeptides. Methods A novel MOAC affinity probe, denoted as G@PDA@ZrO2, was successfully synthesized by in situ grafting ZrO2 onto the surface of graphene (G) modified with polydopamine (PDA). The novel MOAC probe thus obtained was used for phosphopeptide enrichment. Results This novel MOAC affinity probe when used to selectively enrich phosphopeptides from standard protein digest solutions exhibited a high selectivity (β‐casein:bovine serum albumin = 1:1000), a low detection limit (4 fmol), and a high loading capacity (400 mg/g). At the same time, the experimental results proved that G@PDA@ZrO2 had great recyclability (five cycles), stability, and reproducibility. Subsequently, G@PDA@ZrO2 was applied to enrich phosphopeptides from human saliva and human serum, in which 25 and 4 phosphopeptide peaks, respectively, were detected. Conclusions This novel MOAC affinity probe (G@PDA@ZrO2) showed good performance in enriching phosphopeptides. Thus, G@PDA@ZrO2 has good potential in phosphopeptidomics analysis.

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Nickel‐ion substituted hydroxyapatite matrices for metal‐affinity chromatographic purification of recombinant proteins

Ashokan,

Kumar,

Jayaraman

2024

J of Separation Science

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Hydroxyapatite (HAp) is a calcium phosphate ceramic, widely used as a matrix for protein chromatography. The crystal structure of HAp is amenable to a wide range of substitutions, thus allowing for the alteration of its properties. In this study, nickel‐ion substituted HAp (NiSHAp) was synthesized using a wet‐precipitation method, followed by spray drying. This resulted in the structural incorporation of nickel ions within well‐defined microspheres, which were suitable for chromatographic applications. The chromatographic experiments were conducted with NiSHAp and compared with spray‐dried hydroxyapatite (SHAp) matrices. Protein purification experiments were conducted using refolded recombinant L‐asparaginase (L‐Asp), which was produced as inclusion bodies in Escherichia coli. The results showed that NiSHAp effectively adsorbed L‐Asp, which was selectively eluted using a phosphate buffer, surpassing the efficiency of imidazole‐based elution. In contrast, SHAp showed weaker binding and lower selectivity. The significance of this study lies in developing a scalable NiSHAp matrix for protein purification, especially for large‐scale applications. The NiSHAp matrix offers a cost‐effective alternative to commercial immobilized metal affinity chromatography (IMAC) adsorbents, especially for purifying His‐tagged proteins. This innovative approach exhibits the advantages of mixed‐mode chromatography by combining the properties of hydroxyapatite and IMAC in a single matrix, with the potential of improved industrial‐scale protein purification.

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Ni(II)-decorated porous titania microspheres as a stationary phase for column chromatography applications: Highly selective purification of hemoglobin from human blood

Cited by 32 publications

References 34 publications

Recent trends in sorbents for bioaffinity chromatography

Recent trends in sorbents for bioaffinity chromatography

In situ synthesis of a novel metal oxide affinity chromatography affinity probe for the selective enrichment of low‐abundance phosphopeptides

Nickel‐ion substituted hydroxyapatite matrices for metal‐affinity chromatographic purification of recombinant proteins

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