Immobilization and surface characterization of NeutrAvidin biotin-binding protein on different hydrogel interlayers

Vermette, Patrick; Gengenbach, Thomas R.; Divisekera, Upulie; Kambouris, Peter; Griesser, Hans J.; Meagher, Laurence

doi:10.1016/s0021-9797(02)00185-6

Cited by 94 publications

(84 citation statements)

References 49 publications

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“…25 The reaction was allowed to proceed overnight at room temperature. To remove any proteins not linked to PEG-biotin (i.e., NeutrAvidin molecules that can be loosely adsorbed onto the PEG layer), samples were rinsed overnight in a 10 mM HEPES solution, with the solution changed twice.…”

Section: Immobilization Of Liposomesmentioning

confidence: 99%

Fabrication and characterization of contact lenses bearing surface‐immobilized layers of intact liposomes

Danion

Brochu

Martin

et al. 2007

J Biomedical Materials Res

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Intact liposomes were immobilized onto soft contact lenses. In the first step, polyethylenimine was covalently bounded onto the hydroxyl groups available on the surface of a commercial contact lens (Hioxifilcon B). Then, NHS-PEG-biotin molecules were bounded onto the surface amine groups by carbodiimide chemistry. NeutrAvidin were bounded onto the PEG-biotin layer. Liposomes containing PEG-biotinylated lipids were docked onto the surface-immobilized NeutrAvidin. Consecutive addition of further NeutrAvidin and liposome layers enabled fabrication of multilayers. Multilayers of liposomes were also produced by exposing contact lenses coated with NeutrAvidin to liposome aggregates produced by the addition of free biotin in solution. XPS revealed the immobilization of the different layers. By blocking with excess biotin surface-immobilized NeutrAvidin on contact lenses bearing PEG-biotin layers produced under cloud point conditions, ELISA showed that the docking of NeutrAvidin was dependent on biotin-NeutrAvidin affinity binding, with little evidence for nonspecific physisorption; however, it was not possible to differentiate specific versus nonspecific binding of NeutrAvidin attached onto PEG-biotin layers grafted without cloud point conditions. AFM imaging revealed liposome sizes of 106 and 155 nm for layers of liposomes produced (i) by the consecutive addition of further NeutrAvidin and liposomes and (ii) by the exposure of NeutrAvidin-coated contact lenses to liposome aggregates, respectively. The release kinetics of a fluorescent dye demonstrated that intact liposomes had been immobilized onto contact lens surfaces. The stability of surface-immobilized liposomes onto contact lens surfaces showed temperature dependence. Surface-bound liposomes can be stored up to 1 month at 4 degrees C with little release of their content.

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Section: Immobilization Of Liposomesmentioning

confidence: 99%

Fabrication and characterization of contact lenses bearing surface‐immobilized layers of intact liposomes

Danion

Brochu

Martin

et al. 2007

J Biomedical Materials Res

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“…The carbodiimide-immobilized NeutrAvidin barely lost its biotin binding ability when compared to the control sample, indicating that the lysine residues involved in the reaction were not situated close to the binding pockets. [12] The carbodiimide coupling strategy resulted in a greater amount of biotinylated molecules bound to the material surfaces when compared to the affinity ''docking'' strategy, although the non-specific binding background was also higher (up to 70% of the total binding). [12] Silk is a versatile and useful Food and Drug Administration (FDA) approved biomaterial that can be utilized for controlled drug release due to its self-assembly into materials, formation of materials with high mechanical strength, extensive natural physical cross linking, and fairly slow enzymatic degradation in vivo.…”

Section: Introductionmentioning

confidence: 99%

“…[12] The carbodiimide coupling strategy resulted in a greater amount of biotinylated molecules bound to the material surfaces when compared to the affinity ''docking'' strategy, although the non-specific binding background was also higher (up to 70% of the total binding). [12] Silk is a versatile and useful Food and Drug Administration (FDA) approved biomaterial that can be utilized for controlled drug release due to its self-assembly into materials, formation of materials with high mechanical strength, extensive natural physical cross linking, and fairly slow enzymatic degradation in vivo. [13] Silk fibroin is the structural protein found in silk fibers which self-assemble into a ß-sheet rich structure.…”

Section: Introductionmentioning

confidence: 99%

“…The strategy has been studied in detail in the literature using two different materials with extensive carboxyl groups on their surfaces. [12] It was also compared with the affinity ''docking'' strategy of using a surfaceattached biotinylated poly(ethylene glycol) that could bind one side of NeutrAvidin, allowing the other side to interact with biotinylated biomolecules. The carbodiimide-immobilized NeutrAvidin barely lost its biotin binding ability when compared to the control sample, indicating that the lysine residues involved in the reaction were not situated close to the binding pockets.…”

Section: Introductionmentioning

confidence: 99%

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Functionalization of Silk Fibroin with NeutrAvidin and Biotin

Wang

Kaplan

2010

Macromolecular Bioscience

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New methods are needed to modify silk biomaterials with bioactive molecules for tissue engineering and drug delivery. In the present study, silk fibroin in solution or in microsphere format was coupled with NeutrAvidin via carbodiimide chemistry. Silk fibroin retained its self-assembly features after reaction. It was found that more than four NeutrAvidin molecules bound to one silk molecule. Non-specific binding of biotin or NeutrAvidin to silk microspheres could be reduced by pre-treatment of the microspheres with BSA or post-treatment with detergent. The NeutrAvidin-coupled silk microspheres were coupled with biotinylated anti-CD3 antibody and the functionalized microspheres were able to specifically bind to the CD3 positive T-lymphocytic cell line Jurkat.

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“…(Note that if functionalizing the surface with single-stranded DNA, this coverage is ideal for hybridization. 37 ) Assuming each NA occupies an area of ∼25 nm 2 (4 nm × 5 nm × 5.6 nm), 38 an ideal, close-packed monolayer would be ∼4 × 10 12 NA/cm 2 . The actual density is likely to be lower, indicating that we are in the monolayer coverage regime.…”

Section: Resultsmentioning

confidence: 99%

Formation of Primary Amines on Silicon Nitride Surfaces: a Direct, Plasma-Based Pathway to Functionalization

et al. 2007

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Silicon nitride is the most commonly used passivation layer in biosensor applications where electronic components must be interfaced with ionic solutions. Unfortunately, the predominant method for functionalizing silicon nitride surfaces, silane chemistry, suffers from a lack of reproducibility. As an alternative, we have developed a silane-free pathway that allows for the direct functionalization of silicon nitride through the creation of primary amines formed by exposure to a radio frequency glow discharge plasma fed with humidified air. The aminated surfaces can then be further functionalized by a variety of methods; here we demonstrate using glutaraldehyde as a bifunctional linker to attach a robust NeutrAvidin (NA) protein layer. Optimal amine formation, based on plasma exposure time, was determined by labeling treated surfaces with an amine-specific fluorinated probe and characterizing the coverage using X-ray photoelectron spectroscopy (XPS). XPS and radiolabeling studies also reveal that plasma-modified surfaces, as compared with silane-modified surfaces, result in similar NA surface coverage, but notably better reproducibility.

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Immobilization and surface characterization of NeutrAvidin biotin-binding protein on different hydrogel interlayers

Cited by 94 publications

References 49 publications

Fabrication and characterization of contact lenses bearing surface‐immobilized layers of intact liposomes

Fabrication and characterization of contact lenses bearing surface‐immobilized layers of intact liposomes

Functionalization of Silk Fibroin with NeutrAvidin and Biotin

Formation of Primary Amines on Silicon Nitride Surfaces: a Direct, Plasma-Based Pathway to Functionalization

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