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Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method
Published on: July 27, 2016
Titanium-based metal-organic framework MIL-125(Ti) for the highly selective isolation and purification of
Zixin Chi1, Xi Wu2, Qiqi Zhang1
1School of Pharmacy, School of Public Health, Shenyang Medical College, Shenyang, P. R. China.
Abstract:
Titanium-based metal-organic framework MIL-125(Ti) was synthesized by the hydrothermal method of terephthalic acid and tetra butyl titanate in N-N,dimethylformamide, and methanol. MIL-125(Ti) was characterized by Fourier-transform infrared spectroscopy, X-ray diffraction, thermogravimetric analysis, nitrogen adsorption-desorption, energy-dispersive X-ray spectroscopy, zeta potential, scanning electron microscope, and transmission electron microscopy. The results showed MIL-125(Ti) could be used as a potential adsorbent for protein separation and purification due to the high specific surface area, high stability, and strong hydrophobicity. As a result, MIL-125(Ti) had adsorption selectivity for immunoglobulin G, which was due to the hydrogen bond between MIL-125(Ti) and protein. At pH 8.0, the maximum adsorption efficiency of 0.25 mg MIL-125(Ti) for 300 μL 100 μg/mL immunoglobulin G was 98.3%, and its maximum adsorption capacity was 232.56 mg/g. The elution efficiency of immunoglobulin G was 92.4% by 0.1% sodium dodecyl sulfate. sodium dodecyl sulfate-polyacrylamide gel electrophoresis result demonstrated the successful isolation of highly purified immunoglobulin G from the human serum. Therefore, a new method of separation and purification of immunoglobulin G in human serum using titanium-based metal-organic framework MIL-125(Ti) as a solid-phase adsorbent was established, which broadened the application scope of metal-organic frameworks.

