Salt-induced immobilization of affinity ligands onto epoxide-activated supports

Wheatley, Jeffrey B.; Schmidt, Donald E.

doi:10.1016/s0021-9673(99)00484-7

Cited by 117 publications

(85 citation statements)

References 22 publications

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“…It has, however, been reported that soluble proteins are scarcely reactive with epoxy-activated supports even under slightly alkaline conditions [15][16][17][18] . At first glance, this extremely low intermolecular reactivity between epoxy groups and nucleophiles on the protein surface constitutes a serious drawback of monofunctional epoxy supports as supports for single enzyme immobilization protocols and for more interesting enzyme immobilization-stabilization protocols.…”

Section: Immobilization Of Proteins On Monofunctional Epoxy Supportsmentioning

confidence: 99%

“…At high ionic strength, adsorption through the external hydrophobic pockets of the proteins occurs, allowing covalent attachment between nucleophiles and epoxy groups [15][16][17][18] . In fact, this kind of two-step immobilization using hydrophobic supports has already been reported for many enzymes 11,12 .…”

Section: Multipoint Covalent Immobilization Of Proteins On Heterofuncmentioning

confidence: 99%

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Immobilization of enzymes on heterofunctional epoxy supports

et al. 2007

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Section: Immobilization Of Proteins On Monofunctional Epoxy Supportsmentioning

confidence: 99%

Section: Multipoint Covalent Immobilization Of Proteins On Heterofuncmentioning

confidence: 99%

Immobilization of enzymes on heterofunctional epoxy supports

et al. 2007

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“…32,34 Then, the sample was immersed in sericin or collagen solution and shaken for 1 week at room temperature. It has been reported that dermal sheep collagen can be cross-linked by epoxy compound at mild condition for a long time.…”

Section: Processing In An Aqueous Solutionmentioning

confidence: 99%

“…This epoxy compound is chosen here, because the epoxy group existing at the end of the chain is bared on the surface of the PET fabric and acts as a reactive site for functional nucleophilic reagents, including proteins, polysaccharides, nucleic acids, and various small molecules. 34 On the basis of the aforementioned considerations, we tried to modify the surface of PET fabric with natural functional agents (sericin, collagen, or chitosan). In this study, the impregnation of GPE into PET fabric was investigated under various supercritical conditions, in pure CO 2 as well as in CO 2 with a cosolvent, by measuring the mass uptake.…”

Section: Introductionmentioning

confidence: 99%

A novel method of modifying poly(ethylene terephthalate) fabric using supercritical carbon dioxide

Ma¹,

Zhao²,

Okubayashi³

et al. 2010

J of Applied Polymer Sci

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For the modification of poly(ethylene terephthalate) (PET) fabric, a type of epoxy compound, glycerol polyglycidyl ether (GPE), was impregnated as a cross-linking agent into PET fabric by means of supercritical carbon dioxide (scCO 2 ), then, a series of immobilization processes were implemented, including the pad-drycure process and the solution process to finish the GPE-PET fabric with natural functional agents (sericin, collagen, or chitosan). Chloroform was found to be an effective cosolvent, as evidenced by the mass transfer of GPE to PET during the treatment with scCO 2 . Chemical analyses by X-ray photoelectron spectroscopy (XPS) and Fourier transform infrared spectroscopy showed that GPE can penetrate the surface of the PET fabric in scCO 2 pretreatment process, and natural functional agents (sericin, collagen, or chitosan) can also be immobilized on the surface of the GPE-PET fabric especially for the method of pad-drycure. The nitrogen content in the modified PET fabrics was calculated accurately and confirmed by combustion analysis. The modified PET fabric displayed improvements in surface wettability, moisturization efficiency, and antibacterial characteristics against S. aureus, which demonstrated that the feasibility of this design for immobilizing natural functional agents (sericin, collagen, or chitosan) onto the surface of the PET fabric.

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“…It is well known epoxy groups are stable and not very reactive under mild experimental conditions. However, it has also been found that high concentrations of salt facilitate protein immobilization on epoxy-functionalized chromatographic supports [35,36] . In the hypothesized mechanism, hydrophobic interactions are enhanced in the presence of high-concentration salt.…”

Section: Protein Immobilization On Epoxysilane-modifi Ed Silica Nanopmentioning

confidence: 99%

One-step and high-density protein immobilization on epoxysilane-modified silica nanoparticles

2009

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Silica nanoparticles are most commonly modified with amino-silanes, followed by post-modification activation for protein immobilization. In this work, epoxy-functionalized silica nanoparticles were prepared by modification with glycidyloxypropyl trimethoxysilane (GPTMS) for direct protein immobilization. Silica nanoparticles possessed an average size of 46 nm, but increased to 63 nm after GPTMS modification. Reaction time, reaction temperature and GPTMS content had no significant effect on particle size. Zeta potential of SiO 2 changed from −26mV to +38mV after modification. Fourier-transformed infrared spectroscopy revealed alkyl C-H bending and stretching bands at 2944 cm −1 , 1343 cm −1 and 1465 cm −1 , respectively, for the modified nanoparticles. Fluorescein cadaverine was found to bind to GPTMS-modified SiO 2 , but not to bare SiO 2 , indicating the chemical reactivity of epoxy groups on the modified nanoparticle with amines. Finally, fluorescently labeled bovine serum albumin (BSA) was used as a model protein to investigate the capacity of epoxy-SiO 2 nanoparticles for protein immobilization. The results showed that more proteins were immobilized on the particle with longer reaction time, higher NaCl concentration, lower pH, and less GPTMS content. More importantly, proteins bound to epoxy-SiO 2 nanoparticle were highly stable. Under optimized reaction conditions, as much as 25 mg BSA/g nanoparticle was covalently attached to the nanoparticle. The epoxy silane modification of silica nanoparticles offers a reactive surface for one-step and high-density protein immobilization. epoxysilane, silica nanoparticle, protein immobilizationIn the past few years, nanomaterials of various shapes (particles, wires, rods, tubes, etc.) have been synthesized and characterized. They have been found to possess unique size-dependent properties in terms of quantum effect, specific surface area, electric conductivity, mechanical strength, and catalytic reactivity [1] . Consequently, nanomaterials have been found wide applications in the field of biological analysis and detection, biological imaging and drug delivery [2,3] . Among them, silica nanoparticles have been studied extensively due to their easy synthesis, readily available surface modification, good dispersibility and stability in water, and biocompatibility [4] . Mesoporous silica nanoparticles can be employed as drug delivery vehicles for controlled release [5] . Surface-coated silica nanoparticles act as a carrier for multiple optical [6,7] and electrochemical [8] labels to enhance detection signal. Dye-doped silica nanoparticles are more resistant to photo-bleaching than fluorescent dye molecules and much less toxic than quantum dots. They therefore offer distinct advantages when applied to in vivo fluorescence imaging [9,10] . Ruthenium tris(bipyridyl)-doped silica nanoparticles [11][12][13] have been used as electrochemiluminescent labels to provide large quantities of Ru(bpy) 3 2+ molecules for signal detection. Furthermore, silica coating on other

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Salt-induced immobilization of affinity ligands onto epoxide-activated supports

Cited by 117 publications

References 22 publications

Immobilization of enzymes on heterofunctional epoxy supports

Immobilization of enzymes on heterofunctional epoxy supports

A novel method of modifying poly(ethylene terephthalate) fabric using supercritical carbon dioxide

One-step and high-density protein immobilization on epoxysilane-modified silica nanoparticles

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