Characterization of silanization and antibody immobilization on spin-on glass (SOG) surface

Nagare, Gajanan; Mukherji, Soumyo

doi:10.1016/j.apsusc.2008.10.033

Cited by 21 publications

(13 citation statements)

References 14 publications

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“…Fundamental issues in the improvement of the antibodyeantigen interaction are optimised antibody immobilisation and antigen capture efficiency [18,19]. Immobilized antibodies on a porous polymer surface utilise the binding specificity of antibodyeantigen pairing to remove biotoxin.…”

Section: Introductionmentioning

confidence: 99%

Affinity binding of antibodies to supermacroporous cryogel adsorbents with immobilized protein A for removal of anthrax toxin protective antigen

et al. 2015

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Polymeric cryogels are efficient carriers for the immobilization of biomolecules because of their unique macroporous structure, permeability, mechanical stability and different surface chemical functionalities. The aim of the study was to demonstrate the potential use of macroporous monolithic cryogels for biotoxin removal using anthrax toxin protective antigen (PA), the central cell-binding component of the anthrax exotoxins, and covalent immobilization of monoclonal antibodies. The affinity ligand (protein A) was chemically coupled to the reactive hydroxyl and epoxy-derivatized monolithic cryogels and the binding efficiencies of protein A, monoclonal antibodies to the cryogel column were determined. Our results show differences in the binding capacity of protein A as well as monoclonal antibodies to the cryogel adsorbents caused by ligand concentrations, physical properties and morphology of surface matrices. The cytotoxicity potential of the cryogels was determined by an in vitro viability assay using V79 lung fibroblast as a model cell and the results reveal that the cryogels are non-cytotoxic. Finally, the adsorptive capacities of PA from phosphate buffered saline (PBS) were evaluated towards a non-glycosylated, plant-derived human monoclonal antibody (PANG) and a glycosylated human monoclonal antibody (Valortim(®)), both of which were covalently attached via protein A immobilization. Optimal binding capacities of 108 and 117 mg/g of antibody to the adsorbent were observed for PANG attached poly(acrylamide-allyl glycidyl ether) [poly(AAm-AGE)] and Valortim(®) attached poly(AAm-AGE) cryogels, respectively, This indicated that glycosylation status of Valortim(®) antibody could significantly increase (8%) its binding capacity relative to the PANG antibody on poly(AAm-AGE)-protien-A column (p < 0.05). The amounts of PA which remained in the solution after passing PA spiked PBS through PANG or Valortim bound poly(AAm-AGE) cryogel were significantly (p < 0.05) decreased relative to the amount of PA remained in the solution after passing through unmodified as well as protein A modified poly(AAm-AGE) cryogel columns, indicates efficient PA removal from spiked PBS over 60 min of circulation. The high adsorption capacity towards anthrax toxin PA of the cryogel adsorbents indicated potential application of these materials for treatment of Bacillus anthracis infection.

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Section: Introductionmentioning

confidence: 99%

Affinity binding of antibodies to supermacroporous cryogel adsorbents with immobilized protein A for removal of anthrax toxin protective antigen

et al. 2015

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“…5c) therewith indicating an increased surface hydrophobicity possibly due to the protruding free amino groups of APTES. 40,41 Glutaraldehyde treatment preceding the silanization decreases the contact angle to 43.367 ( Fig. 5d).…”

Section: Characterization Of Immunoassay Matrixmentioning

confidence: 94%

Development and evaluation of an IgY based silica matrix immunoassay platform for rapid onsite SEB detection

et al. 2018

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“…However, according to Nagare and Mukherji (2009), the present preparation of the APTES solution at pH 5 may promote the amine group density of the silane. This condition, added to the MAb carboxyl group activation by EDC/NHS, could explain the immobilisation difference when APTES or GPTMS were used for the surface modification.…”

Section: Electrode Activity Testingmentioning

confidence: 98%

Characterisation of electrochemical immunosensor for detection of viable not-culturable forms of Legionellla pneumophila in water samples

et al. 2015

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Legionella pneumophila may cause a fatal pneumonia in humans known as Legionnaires' disease (LD). The strategies of L. pneumophila to adapt to and resist stressful environmental conditions include the ability to enter into a VBNC (viable but not culturable) state. The detection of L. pneumophila in environmental samples benefits from the use of standardised methods: for detection and enumeration following membrane filtration (AFNOR T90-431, ISO 11731) and detection and quantification by polymerase chain reaction PCR (AFNOR T90-471, ISO 12869). Culture is hampered by its inability to detect VBNC forms and PCR is unable to discriminate between live and dead bacteria. The present immunosensor was obtained by the immobilisation of a monoclonal anti-L. pneumophila antibody (MAb) on an indium-tin oxide (ITO) electrode by the self-assembled monolayers (SAMs) method using an aminosilane. The immunosensor was characterised by wettability (contact angle measurement), atomic force microscopy (AFM), confocal laser scanning microscopy (CLSM), and electrochemical impedance spectroscopy (EIS). A limit of detection of 10 bacteria per mL was observed on artificial samples.

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Characterization of silanization and antibody immobilization on spin-on glass (SOG) surface

Cited by 21 publications

References 14 publications

Affinity binding of antibodies to supermacroporous cryogel adsorbents with immobilized protein A for removal of anthrax toxin protective antigen

Affinity binding of antibodies to supermacroporous cryogel adsorbents with immobilized protein A for removal of anthrax toxin protective antigen

Development and evaluation of an IgY based silica matrix immunoassay platform for rapid onsite SEB detection

Characterisation of electrochemical immunosensor for detection of viable not-culturable forms of Legionellla pneumophila in water samples

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