Poly(glycidyl methacrylate)‐grafted hydrophobic charge‐induction agarose resins with 5‐aminobenzimidazole as a functional ligand

Liu, Tao; Lin, Dong‐Qiang; Wang, Cun-Xiang; Yao, Shan-Jing

doi:10.1002/jssc.201600482

Cited by 10 publications

(4 citation statements)

References 30 publications

(61 reference statements)

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“…Liu et al. modified the above mentioned preparation protocol further by grafting poly(glycidyl methacrylate) on agarose resin with subsequent coupling of 5‐aminobenzimidazole as a functional ligand . Adsorption isotherms, kinetics, and dynamic binding behavior of the resulting resins were investigated using human IgG as a model protein, and the effect of ligand density was evaluated.…”

Section: Polymeric Mixed‐mode Stationary Phasesmentioning

confidence: 99%

Recent advances in mixed‐mode chromatographic stationary phases

Sýkora

Řezanka

Záruba

et al. 2018

J of Separation Science

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Mixed‐mode phases have become very popular in the last decade, and the number of new mixed/multi‐mode sorbents is growing fast. Unlike single‐mode stationary phases, perfectly suited for the separation of the analytes possessing similar physicochemical properties, for instance reversed‐phase chromatography for hydrophobic solutes, mixed‐mode sorbents providing multimodal interactions can render better separation selectivity for complex mixtures of solutes differing significantly in their physicochemical characteristics. The most frequent modern mixed‐mode stationary phases are di/tri‐mode sorbents embracing the following interactions, hydrophobic, electrostatic (coulombic), and hydrophilic. According to their structures, it is possible to distinguish silica‐based, polymer‐based, hybrid, and monolithic mixed‐mode stationary phases. Herewith, newly synthesized mixed‐mode sorbents developed within the last two and half years are categorized, discussed, and summarized. The main attention is devoted to the description of the synthetic routes and characterization methods applied for the new stationary phases.

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Section: Polymeric Mixed‐mode Stationary Phasesmentioning

confidence: 99%

Recent advances in mixed‐mode chromatographic stationary phases

Sýkora

Řezanka

Záruba

et al. 2018

J of Separation Science

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“…Cation exchanger SP Sepharose FF showed high capacity but poor selectivity and salt tolerance, and fermentation broth needed to be diluted before adsorption [9]. Mixed‐mode chromatography is a novel technology for protein separation [10–12], and mixed‐mode resin CST‐II FF showed salt tolerance but low selectivity [13]. Capto MMC was used to separate rHSA from rice seeds extract, but the selectivity was also limited [14].…”

Section: Introductionmentioning

confidence: 99%

Rational design of specific ligands for human serum albumin separation and applications

Cai

Zhang

et al. 2020

J of Separation Science

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Human serum albumin is widely used in clinical practice, and the development of new ligands with high affinity is beneficial to improve its separation efficiency. The Site II of human serum albumin is an active binding site of various molecules such as l‐tryptophan, which was studied with molecular simulation to obtain insights for the design of new ligands. The results showed that the carboxyl and indolyl groups of l‐tryptophan were critical for the binding on Site II. Seven ligands containing carboxyl groups and indolyl groups were designed, and molecular simulation showed that indole‐3‐pentanoic acid was the best ligand. A new ligand combined indole‐3‐acetic acid and cysteine was designed for easier resin preparation, and molecular simulation also indicated that the new ligand bound strongly to Site II. Resins with the new ligand designed was prepared and static adsorption experiments indicated that the new resin had high adsorption capacity of human serum albumin and strong salt tolerance. Finally, recombinant human serum albumin was separated from yeast broth with high purity of 90.4% and recovery of 94.2%, which indicated that the new resin had good adsorption selectivity and strong potential for applications.

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Section: Introductionmentioning

confidence: 99%

“…And compared to the nongrafted resins, the dextran-grafted layer on the resin could increase the ligand density, enhance the mass transport in the pore, and improve the dynamic adsorption at high kinetics. In the further research, Liu et al have prepared new poly(glycidyl methacrylate)-grafted hydrophobic charge-induction resins with 5-aminobenzimidazole as the functional ligand. The results showed that the resins with the ligand density of 330 μmol/g (G-ABI-330 resin) had the maximum adsorption capacity and binding affinity for hIgG, which were better than the HCIC resins reported in the literature. , Moreover, the dynamic binding capacity value at 10% breakthrough of the G-ABI-330 resins could reach to 76.3 mg/g at linear velocity 300 cm/h, which was also higher than those of nongrafted resins and other polymer-grafted HCIC resin (G-MMI and MMI-B-XL-200). , It is obvious that suitable polymers grafted to the resins could improve the binding ability between chromatographic resins and antibody.…”

Section: Introductionmentioning

confidence: 99%

Adsorption of IgG and BSA on Two Chromatographic Resins—Poly(ethylenimine)-4FF Resin and Tetrapeptide-poly(ethylenimine)-4FF Resin

2018

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Poly(ethylenimine) (PEI) as a long flexible chain has been well used in protein chromatography with the advantages of high spatial utilization and “chain delivery” effect. In this work, two resins, i.e., poly(ethylenimine)-4FF resin (PEI-4FF resin) and Ac-YFRH-PEI-4FF resin by grafting tetrapeptide to PEI-4FF resin, were prepared for the protein adsorption and chromatographic separation. The pH-dependent adsorption properties of PEI-4FF resin and Ac-YFRH-PEI-4FF resin were discovered by getting the data of adsorption capacities of bovine serum albumin (BSA) and immunoglobulin G (IgG) under different pH conditions and buffer systems. The results showed high binding capacities of BSA on PEI-4FF resins across a range of pH values (5.0–8.9) with almost very little adsorption of IgG over a pH range from 5.0 to 8.0, indicating that IgG could be separated by flow-through method using PEI-4FF resin. Since PEI has the advantage of having many flexible branched chains and Ac-YFRH (Ac-Try-Phe-Arg-His) as a peptide ligand has the advantages of comparatively high stability and low immunogenicity for antibody adsorption, Ac-YFRH-PEI-4FF resins were prepared by using PEI as the spacer arm and Ac-YFRH as the peptide ligand. The isotherm adsorption of the Ac-YFRH-PEI-4FF resin showed that the maximum binding capacity of IgG (q m = 123.6 mg/g resin, K d = 0.10 mg/mL) was far more than that of BSA (q m = 62.0 mg/g resin, K d = 0.25 mg/mL) at pH 8.0. Meanwhile, this tetrapeptide resin also showed high binding capacity of BSA (q m = 131.0 mg/g resin, K d = 0.05 mg/mL) and low binding capacity of IgG (q m = 2.0 mg/g resin, K d = 0.01 mg/mL) at pH 5.0, indicating that the separation of BSA and IgG could be achieved with the big differences in adsorption behaviors.

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Poly(glycidyl methacrylate)‐grafted hydrophobic charge‐induction agarose resins with 5‐aminobenzimidazole as a functional ligand

Cited by 10 publications

References 30 publications

Recent advances in mixed‐mode chromatographic stationary phases

Recent advances in mixed‐mode chromatographic stationary phases

Rational design of specific ligands for human serum albumin separation and applications

Adsorption of IgG and BSA on Two Chromatographic Resins—Poly(ethylenimine)-4FF Resin and Tetrapeptide-poly(ethylenimine)-4FF Resin

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