Effect of carboxyl density at the core–shell interface of surface-imprinted magnetic trilayer microspheres on recognition properties of proteins

Li, Xiangjie; Zhang, Baoliang; Tian, Lei; Li, Wei; Xin, Tiejun; Zhang, Hepeng; Zhang, Qiuyu

doi:10.1016/j.snb.2014.01.109

Cited by 25 publications

(15 citation statements)

References 25 publications

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“…Therefore, this approach is well suited for imprinting of biomacromolecules like proteins . Depending on application modes, the solid supports subjected to surface imprinting of proteins can be nanomaterials , electrodes , microspheres , membranes , and monoliths. Molecular imprinting of proteins in polymers attached to the surface of nanomaterials is currently a hot topic; however, this application mainly focuses on the fabrication of biosensors since the nanomaterials exhibit a remarkably large surface‐to‐volume ratio and size‐related physical and chemical properties.…”

Section: Introductionmentioning

confidence: 99%

“Smart” molecularly imprinted monoliths for the selective capture and easy release of proteins

Wen

Tan

Sun

et al. 2016

J of Separation Science

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A new thermally switchable molecularly imprinted monolith for the selective capture and release of proteins has been designed. First, a generic poly(glycidyl methacrylate-co-ethylene dimethacrylate) monolith reacted with ethylenediamine followed by functionalization with 2-bromoisobutyryl bromide to introduce the initiator for atom transfer radical polymerization. Subsequently, a protein-imprinted poly(N-isopropylacrylamide) layer was grafted onto the surface of the monolithic matrix by atom transfer radical polymerization. Scanning electron microscopy and energy-dispersive X-ray spectroscopy of the cross-sections of imprinted monoliths confirmed the formation of dense poly(N-isopropylacrylamide) brushes on the pore surface. The imprinted monolith exhibited high specificity and selectivity toward its template protein myoglobin over competing proteins and a remarkably large maximum adsorption capacity of 1641 mg/g. Moreover, this "smart" imprinted monolith featured thermally responsive characteristics that enabled selective capture and easy release of proteins triggered only by change in temperature with water as the mobile phase and avoided use of stronger organic solvents or change in ionic strength and pH.

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Section: Introductionmentioning

confidence: 99%

“Smart” molecularly imprinted monoliths for the selective capture and easy release of proteins

Wen

Tan

Sun

et al. 2016

J of Separation Science

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“…[21][22][23] Furthermore, the synthesis process was usually performed in organic solvents, which is a minus point for protein imprinting. [21][22][23] Furthermore, the synthesis process was usually performed in organic solvents, which is a minus point for protein imprinting.…”

Section: Introductionmentioning

confidence: 99%

Specific removal of protein using protein imprinted polydopamine shells on modified amino-functionalized magnetic nanoparticles

et al. 2014

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Thin imprinting shell over functionalized magnetic nanoparticles is an effective solution to weaken mass transfer resistance, achieve high binding capacity, and attain rapid separation. In this work, a simple, green, and resultful approach was developed to imprint bovine serum albumin (BSA) on the surface of amino-modified Fe 3 O 4 nanoparticles (Fe 3 O 4 @NH 2 ) using dopamine as monomer through a two-step immobilized template strategy. The results of X-ray diffraction and vibrating sample magnetometer indicated that the as-synthesized nanomaterials exhibited high crystallinity and satisfactory superparamagnetic properties. Transmission electronic microscopy and Fourier transform infrared spectroscopy of the products showed that polydopamine shells successfully attached onto Fe 3 O 4 @NH 2 . The polydopamine shells with a thickness of about 10 nm enables the template recognition sites to be accessed easily, and exhibits fast kinetics and high adsorption capacity in aqueous solution. Meanwhile, a excellent selectivity towards BSA had been presented when employed bovine hemoglobin (BHb), transferrin, and immunoglobulin G (Ig G) as competitive proteins. Good recovery after a reasonably mild elution and successful capture of the target protein from a real sample of bovine blood suggested its potential value in practical applications. In addition, the resultant polymers were stable and had no obvious deterioration after at least six adsorption-regeneration cycles. The versatility of the proposed method had also been verified by choosing four other proteins with different isoelectric points as the templates. of adsorption were measured by using a UV-2450 spectrophotometer (Shimadzu, Japan). Electrophoretic analysis of protein samples was performed using regular SDS-PAGE (Bio-Rad, Hercules, CA) with 10% running and 5% stacking gels.Proteins were stained with Coomasie Brilliant Blue R-250. @NIPs were incubated in 10 mL of Tris-HCl (10 mM, pH = 7.0) solution of BSA, BHb, Hb, RNase A, and Lyz at a concentration of 0.30 mg mL -1 respectively at room temperature for 20 min. (n = 5)

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“…Each MCNC is composed of plentiful interconnected primary Fe 3 O 4 nanocrystals of $10 nm in size together with minor amount of organic components, which render the resulting clusters superparamagnetism and also high-magnetization. Several research groups have employed MCNCs or MCNCs based core-shell microspheres as support materials to construct magnetically recyclable surface protein-imprinted microspheres [16,17,28,29].…”

Section: Resultsmentioning

confidence: 99%

“…S3), which may explain the great the specific rebinding difference aforementioned. Recently, Li et al also proved that the imprinting performance of coreshell Lyz or BSA-imprinted particles increases with increasing the carboxyl density within a certain range on the surface of the core microspheres [17].…”

Section: Rebinding Propertiesmentioning

confidence: 99%

“…Template molecules can be immobilized on the surface via either reversible covalent bonding (like imine bond and phenylboronic acid ester), or affinity interactions such as those based on an enzyme and its inhibitor [10][11][12][13][14]. Also, the template proteins can be physically adsorbed on the surface of the supports modified with suitable functional groups [15][16][17][18][19]. The latter strategy based on physical uptake has been more widely employed due to much easier surface functionalization and subsequent template removal in contrast with the covalent template immobilization approach.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Enhanced surface imprinting of lysozyme over a new kind of magnetic chitosan submicrospheres

Guo

Yuan

2015

Journal of Colloid and Interface Science

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Effect of carboxyl density at the core–shell interface of surface-imprinted magnetic trilayer microspheres on recognition properties of proteins

Cited by 25 publications

References 25 publications

“Smart” molecularly imprinted monoliths for the selective capture and easy release of proteins

“Smart” molecularly imprinted monoliths for the selective capture and easy release of proteins

Specific removal of protein using protein imprinted polydopamine shells on modified amino-functionalized magnetic nanoparticles

Enhanced surface imprinting of lysozyme over a new kind of magnetic chitosan submicrospheres

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