The reduced adsorption of lysozyme at the phosphorylcholine incorporated polymer/aqueous solution interface studied by spectroscopic ellipsometry

Murphy, Emma F.; Keddie, Joseph L.; Lu, Jian R.; Brewer, J. R.; Russell, Jeremy C.

doi:10.1016/s0142-9612(99)00059-9

Cited by 44 publications

(39 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In comparison, omafilcon A is a neutral, FDA group II hydrogel comprised of polyHEMA and the biocompatible monomer phosphorylcholine. 48 -51 Phosphorylcholine has been shown to be highly resistant to protein deposition in both hydrogel membranes 48,52,53 and when fabricated into contact lenses, 54,55 and the data from this study further show that phosphorylcholine-based contact lens materials acquire relatively low levels of protein deposit.…”

Section: Discussionmentioning

confidence: 59%

Quantity and Conformation of Lysozyme Deposited on Conventional and Silicone Hydrogel Contact Lens Materials Using an In Vitro Model

Suwala

Glasier

Subbaraman

et al. 2007

Eye &Amp; Contact Lens: Science &Amp; Clinical Practice

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 59%

Quantity and Conformation of Lysozyme Deposited on Conventional and Silicone Hydrogel Contact Lens Materials Using an In Vitro Model

Suwala

Glasier

Subbaraman

et al. 2007

Eye &Amp; Contact Lens: Science &Amp; Clinical Practice

View full text Add to dashboard Cite

show abstract

“…To avoid the coupling problem, we have tried to fix the refractive index of the protein layer close to that of the pure protein. We have demonstrated that this approach has little effect on the surface excess [24]. Following the previous work by De Feitjer [17], the surface excess ( in mg m −2 ) can be estimated from the following equation:…”

Section: Spectroscopic Ellipsometrymentioning

confidence: 84%

“…We have explained previously that for the formation of an ultrathin interfacial layer, SE is incapable of separating the layer thickness from its volume fraction [23,24]. To avoid the coupling problem, we have tried to fix the refractive index of the protein layer close to that of the pure protein.…”

Section: Spectroscopic Ellipsometrymentioning

confidence: 99%

See 1 more Smart Citation

Ab initiocalculations of the physical properties of ionic crystals

2004

View full text Add to dashboard Cite

The Arg-Gly-Asp (RGD) peptide sequence is known as a cell recognition site for numerous adhesive proteins present in the extracellular matrix (ECM) and in blood. Whilst surface immobilized RGD groups enhance cell attachment, RGD components present in solution can effectively inhibit cell attachment by competing with endogenous ligands for the same recognition site. In contrast to the widely reported binding to cell integrin, this study demonstrates a new RGD feature: its inhibitive effect on fibrinogen adsorption. Through a combined analysis of spectroscopic ellipsometry, neutron reflection and dual polarization interferometry, we show that the kinetic process of fibrinogen adsorption as a model pro-coagulant at the silica/solution interface and in the absence of any cells can be substantially reduced by the addition of RGD in solution and that the extent of the reduction is dependent on the relative concentration of RGD.

show abstract

“…This approach has little effect on the surface excess. 24,25 Although SE is incapable of separating the true thickness from its refractive index, it is sufficiently accurate to determine the adsorbed protein amount (Γ in mg/m 2 ), which is proportional to the product of thickness (τ in Å) and refractive index (n). According to the work by De Feitjer et al, 27 Γ can be related to τ and n through the following equation…”

Section: Resultsmentioning

confidence: 99%

Effect of Surface Packing Density of Interfacially Adsorbed Monoclonal Antibody on the Binding of Hormonal Antigen Human Chorionic Gonadotrophin

2006

Self Cite

View full text Add to dashboard Cite

Interfacial adsorption of a mouse monoclonal antibody (type IgG1, anti-beta-hCG) at the hydrophilic silicon oxide/water interface has been studied by spectroscopic ellipsometry and neutron reflection, followed by assessment of binding of a hormonal antigen, human chorionic gonadotrophin (hCG), onto the adsorbed antibody molecules. The amount of adsorption reached a maximum around the isoelectric pH (IP) of 6 for the antibody; this pH-dependent pattern could be altered by increasing salt concentration, a trend also observed for other proteins. Neutron reflection revealed the formation of a 40 A uniform layer from the adsorbed antibody, indicating a flat-on orientation. The subsequent hCG binding showed that the molar ratio of hCG bound to antibody at the interface was as high as 0.7 at low surface coverage of antibody and decreased with increasing surface antibody concentration. The results point to an increasing extent of steric hindrance to hCG access with increasing packing density of antibody molecules on the surface. Comparison with previously published crystal structure studies suggests twisting of the variable region to allow access of the antigen. The binding of hCG was also found to be pH-dependent with its maximum around the IP, if the ionic strength of the solution was low (20 mM). However, if the ionic strength was increased to 200 mM, then hCG binding was influenced by a combination of steric hindrance and electrostatic interaction between the antigen and the surface. These results are highly relevant to the improvement of the performance of biotechnologies such as fertility test pads and biosensors based on antibody immobilization.

show abstract

The reduced adsorption of lysozyme at the phosphorylcholine incorporated polymer/aqueous solution interface studied by spectroscopic ellipsometry

Cited by 44 publications

References 0 publications

Quantity and Conformation of Lysozyme Deposited on Conventional and Silicone Hydrogel Contact Lens Materials Using an In Vitro Model

Quantity and Conformation of Lysozyme Deposited on Conventional and Silicone Hydrogel Contact Lens Materials Using an In Vitro Model

Ab initiocalculations of the physical properties of ionic crystals

Effect of Surface Packing Density of Interfacially Adsorbed Monoclonal Antibody on the Binding of Hormonal Antigen Human Chorionic Gonadotrophin

Contact Info

Product

Resources

About