Citation: CHENG Fang, FENG Qian-Cheng, HE Wei, ZHAO Xian-Ming, WANG Qing. Preparation and Characterization of PEGylated Thiophilic Nanoparticles for Rapid Antibody Separation[J]. Chinese Journal of Analytical Chemistry, ;2018, 46(12): 1953-1960. doi: 10.11895/j.issn.0253-3820.181530 shu

Preparation and Characterization of PEGylated Thiophilic Nanoparticles for Rapid Antibody Separation

CHENG Fang ^1,2, ,
FENG Qian-Cheng ² ,
HE Wei ^1,3 ,
ZHAO Xian-Ming ² ,
WANG Qing ^1,2

1.
State Key Laboratory of Fine Chemicals, Dalian University of Technology, Dalian 116023, China;
2.
School of Pharmaceutical Science and Technology, Dalian University of Technology, Dalian 116023, China;
3.
School of Chemical Engineering, Dalian University of Technology, Dalian 116023, China

Received Date: 13 August 2018
Revised Date: 29 September 2018

Fund Project: This work was supported by the National Natural Science Foundation of China (Nos. 21773022, 31771033) and the Fundamental Research Funds for the Central Universities, China (No. DUT16RC(3)019).

New core-shell structure based magnetic nanoparticles for immunoglobulin separation were prepared, in which thiophilic property of sulfone groups and protein resistance of poly(ethylene glycol) (PEG) moieties were displayed. The step-wise surface reactions on the nanoparticles were characterized by ¹H nuclear magnetic resonance (NMR) and surface Zeta potential measurement. With human immunoglobulin G (human IgG) and bovine serum albumin (BSA) as model proteins, the effects of PEG chain length, conjugation group, solution pH and salt concentration on IgG selectivity were investigated using static adsorption experiments. The experiment results showed that mPEG2000-NH₂ modified magnetic nanoparticles had an adsorption capacity of 132.8 mg/g and selectivity of 32.5 towards IgG under the condition of pH 7.45 and 0.15 mol/L NaCl. In complex biochemical solutions, the PEG modified magnetic nanoparticles could separate IgG from fetal calf serum and Omalizumab from cell culture supernatant with purities of 96% and 99%, respectively. Moreover, the binding affinities of the core-shell structure towards IgG from four species (human, bovine, rabbit and goat) were quantified by bio-layer interferometer. The results showed that the selectivity of this structure towards IgG varied from traditional Protein A method, suggesting its potentials in rapid separation and purification of IgG with low affinity towards Protein A.
- Antibody separation,
- Thiophilic ligand,
- Poly (ethylene glycol),
- Magnetic nanoparticles,
- Vinyl sulfone
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