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Fabrication and characterization of hierarchical porous Ni2+doped hydroxyapatite microspheres and their enhanced protein adsorption capacity

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Chinese Journal of Chemical Engineering 2022年第5期35卷 238-247页

作者： Yaling Li Hao Ai Liangzhi Qiao Yinghong Wang Kaifeng Du Department of Pharmaceutical&Biological Engineering School of Chemical EngineeringSichuan UniversityChengdu 610065China

Hydroxyapatite(HAP)is a common bio-adsorbent,which performance depends heavily upon its morphology and microporous structure.In this study,a novel synthesis strategy was proposed for hierarchical porous HAP microspheres by a simple"one-pot"hydrothermal reaction.In the strategy,L-glutamic acid serves as soft template to modulate the morphology and inner crystalline of HAP.To evaluate the application potential,doping Ni^(2+) on hierarchical porous HAP microspheres gives metal chelated affinity adsorbents.The prepared adsorbents show a perfect spherical shape,particles size of 96.6μm,relatively specific surface area of 48.5 m^(2)·g^(-1) and hierarchical pores(mesopores:4 nm and macropores:53 nm).By the adsorption evaluation,it reveals that the Ni^(2+)-HAP adsorbents have high adsorption capacities of275.11 and 97.55 m^(2)·g^(-1) for hemoglobin and bovine serum albumin,respectively,which is comparable to other similar adsorbent.Therefore,this work provides a promising method for high-efficiency hydroxyapatite microspheres for proteins purification.

关键词： Hierarchical porous hydroxyapatite microspheres Templates Metal doping proteins adsorption

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Interaction of Plasma proteins with Tri-quaternary Ammonium Salt Cationic Surfactant Studied by QCM-D

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中国化学:英文版 2015年第2期33卷 253-260页

作者： Man Xi Baoyan Zhang Research Center for Molecular Science and Engineering Northeastern UniversityShenyangLiaoning 110819China

A tri-quaternary ammonium salt cationic surfactant was synthesized.Its structure was confirmed by using Fourier-transform infrared spectroscopy,^(1)H nuclear magnetic resonance spectroscopy,and X-ray photoelectron spectroscopy analyses.Three model surfaces,including Au-CH_(3),Au-OH and Au-COOH,were fabricated.adsorptions of surfactant on the three model surfaces and subsequent plasma proteins adsorption were investigated by quartz crystal microbalance with dissipation(QCM-D).The mass of surfactant on the Au-COOH surface was the largest,followed by that on the Au-CH_(3)surface,and that on the Au-OH surface.These results suggested that the main driving force of surfactant immobilization was electrostatic interaction followed by hydrophobic interaction.Based on the results obtained,we concluded that the protein mass adsorbed on Au-CH_(3)-S,Au-OH-S,and Au-COOH-S surfaces depended on the protein size and orientation.The mass and thickness of S on the Au-COOH surface is the largest and the protein adsorption capacity of Au-COOH-S surface is inferior to that of Au-CH_(3)-S.The Au-COOH-S surface could inhibit lysozyme adsorption,maintain the adsorption balance of bovine serum albumin,and induce fibrinogen-binding protein adsorption.

关键词： tri-quaternary ammonium salt cationic surfactant self-assembled monolayers quartz crystal micro-balance with dissipation(QCM-D) proteins adsorption

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