Adsorption Mechanism of Acid Pretreated Antibodies on Dichlorodimethylsilane-Treated Silica Surfaces

Chang, I‐Nan; Lin, Jinn-Nan; Andrade, Joseph D.; Herron, James N.

doi:10.1006/jcis.1995.1358

Cited by 30 publications

(46 citation statements)

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“…Thus, with increasing adsorption the ␥-globulin molecules either adapt an orientation more normal to the surface or undergo a smaller conformational change on adsorption. These effects have been illustrated for similar systems by Chang et al (41) and Buijs et al (13) (see also discussion below). Furthermore, crowding-dependent conformational changes have been illustrated previously, e.g., by Kondo and Mihara for hemoglobin and myoglobin adsorbing at various colloidal particles (79) (Fig.…”

Section: "Soft Shape" Proteinsmentioning

confidence: 71%

“…Examples include studies of fibrinogen by Schaaf et al , that acid-pretreated antibodies at hydrophobic surfaces display a significantly increased antigen-binding capacity compared to that of native antibodies (2,41). Most likely, this is a consequence of an increased degree of orientation of the antibodies at the hydrophobic surfaces, since acid treatment is known to cause denaturation of the Fc part of the antibodies, thereby exposing hydrophobic groups and favouring the adsorption of the Fc part at the hydrophobic surface.…”

Section: Effects Of Protein-solvent Interactionsmentioning

confidence: 95%

“…Note, however, that this seems not to be the complete picture. For example, Chang et al found that acid pretreatment of antibodies may increase the degree of accessability of the Fab fragments to antigen binding, which is likely to be coupled to the interfacial orientation of antibodies (41,100). Furthermore, Buijs et al found that IgG's undergo conformational changes on adsorption, depending on both the adsorbed amount and the surface properties (13).…”

Section: Adsorbed Layer Formationmentioning

confidence: 96%

See 2 more Smart Citations

Formation of Adsorbed Protein Layers

Malmsten¹

1998

Journal of Colloid and Interface Science

226

183

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Section: "Soft Shape" Proteinsmentioning

confidence: 71%

Section: Effects Of Protein-solvent Interactionsmentioning

confidence: 95%

Section: Adsorbed Layer Formationmentioning

confidence: 96%

See 1 more Smart Citation

Formation of Adsorbed Protein Layers

Malmsten¹

1998

Journal of Colloid and Interface Science

226

183

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“…It is also known for low pH values that antibodies exhibit hydrophobic regions by conformational change, specifically at the site of the Fcregion, depending on the time of exposure to the acidic environment (Van Erp at al. 1992;Chang et al 1995). This behaviour has been subsequently used for proper immobilization of antibodies on hydrophobic dye doped silica (Chang et al 1995).…”

Section: Effects Of Buffer Ionic Strength On Cementioning

confidence: 99%

“…1992;Chang et al 1995). This behaviour has been subsequently used for proper immobilization of antibodies on hydrophobic dye doped silica (Chang et al 1995).…”

Section: Effects Of Buffer Ionic Strength On Cementioning

confidence: 99%

Evaluation of zero-length cross-linking procedure for immuno-magnetic separation of Leptospira

et al. 2010

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Leptospirosis constitutes a major health problem in tropical and subtropical countries and is caused by pathogenic Leptospira. Immuno-magnetic separation (IMS) is considered to be an effective pre-enrichment method to isolate Leptospira from liquid specimen. We applied an inexpensive and simple IMS protocol using zero-length cross-linkers to immobilize polyclonal anti-leptospiral antibodies onto magnetic particles. The IMS-system has been optimized and evaluated by the assessment of the capture efficiency (CE). Main parameters that influence the conjugation procedure were optimized, including the amount of protein per milligram of magnetic particles, the pH and ionic strength of the conjugation buffer. The bead-bound leptospiral fraction was identified by using acridine orange fluorescence dye. The highest value for CE occurred when using high molar phosphate saline buffer at a pH around the isoelectric point of the antibodies. Finally, up to 3×10 8 leptospiral cells per mL could have been captured with approximately 50 µg of antibody-labelled particles. Strong particle agglutination could be observed during incubation for leptospiral concentrations in the range of 10 7 -10 8 cells per mL. Despite covalent binding, we show that the physical adsorption parameters pH and ionic strength of the conjugation buffer greatly affect the entire immobilization process with regard to the CE, thus being able to increase the reactivity of the particles. We therefore conclude that a well-adjusted conjugation buffer for the used chemistry could possibly replace expensive and more complicated antibody immobilization methods.

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Multivalent Binding of Small Guest Molecules and Proteins to Molecular Printboards inside Microchannels

Ludden

Ling

Tang

et al. 2007

Chemistry A European J

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Beta-Cyclodextrin (beta-CD) monolayers have been immobilized in microchannels. The host-guest interactions on the beta-CD monolayers inside the channels were comparable to the interactions on beta-CD monolayers on planar surfaces, and a divalent fluorescent guest attached with a comparable binding strength. Proteins were attached to these monolayers inside microchannels in a selective manner by employing a strategy that uses streptavidin and orthogonal linker molecules. The design of the chip, which involved a large channel that splits into four smaller channels, allowed the channels to be addressed separately and led to the selective immobilization of antibodies. Experiments with labeled antibodies showed the selective immobilization of these antibodies in the separate channels.

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Adsorption Mechanism of Acid Pretreated Antibodies on Dichlorodimethylsilane-Treated Silica Surfaces

Cited by 30 publications

References 0 publications

Formation of Adsorbed Protein Layers

Formation of Adsorbed Protein Layers

Evaluation of zero-length cross-linking procedure for immuno-magnetic separation of Leptospira

Multivalent Binding of Small Guest Molecules and Proteins to Molecular Printboards inside Microchannels

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