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Polymers surface, protein adsorption

Keywords Assay Bioactive surface Cell adhesion Cell chip Hydrogel Microengineering Micropattern Peptide Polymer brush Protein adsorption... [Pg.35]

Before long-term hemocompatibility can be expected for any material, the nature of polymer surface-protein interaction must be established in more detail the way in which the polymer surface alters itself (rotation of segments, side groups, chain refolding, etc.) in response to the protein species the way the protein is altered in conformation (if at all) upon adsorption by the surface and how this conformational change provokes platelet retention. Of course, longer-term ex vivo or in vivo studies also will be necessary. [Pg.48]

Table 1. Polymer and Protein Adsorption Data Measured with OWLS, Expressed as the Surface Density of PEG Chains and EG Monomers, npEc [nm ], reg [nm ], and the Mass of Adsorbed Serum, nisemm [Ng/ cm ], Standard Deviation ... Table 1. Polymer and Protein Adsorption Data Measured with OWLS, Expressed as the Surface Density of PEG Chains and EG Monomers, npEc [nm ], reg [nm ], and the Mass of Adsorbed Serum, nisemm [Ng/ cm ], Standard Deviation ...
Samples, one half coated with SiOa and the other half with Ti02, were used for quantitative surface analysis after each of the siuface treatment steps (cleaning, self-assembly, and polymer and protein adsorption, section 2). These samples exhibit material contrast on a macroscopic scale and are discussed in section 3.1. Micropat-temed surfaces were subjected to identical siuface modification procedures and characterized qualitatively by imaging ToF-SIMS (section 3.2) and fluorescence microscopy (section 3.3) and were used in the cell experiments (section 3.4). In both types of samples, material contrast (on a macroscopic or microscopic scale, Figure la) is converted into contrast with respect to protein adhesion (Figure Ic) via a series of surface modification steps (self-assembly of DDP, adsorption of PLL-g-PEG section 2). [Pg.555]

The MPC polymers suppressed protein adsorption well. It was reported that the theoretical amounts of BSA and BPF adsorbed on the surface in a monolayered state are 0.9 pg/cra and 1.7 pg/cm, respectively. On the surface of PMB30, the amount of adsorbed proteins was less than these theoretical values. Thus, the phosphorylcholine group is considered to reduce protein adsorption effectively. The effectiveness of the phosphorylcholine group, particularly the MPC unit, for reducing protein adsorption has been reported by other groups. ... [Pg.153]

J. D. Andrade, Surface and Interfacial Aspects of Biomedical Polymers, Vol. 2, Protein Adsorption, Plenum, 1985. [Pg.425]

Biomaterials with Low Thrombogenicity. Poly(ethylene oxide) exhibits extraordinary inertness toward most proteins and biological macromolecules. The polymer is therefore used in bulk and surface modification of biomaterials to develop antithrombogenic surfaces for blood contacting materials. Such modified surfaces result in reduced concentrations of ceU adhesion and protein adsorption when compared to the nonmodifted surfaces. [Pg.344]

RAIRS is routinely used for the analysis of chemically modified surfaces - surface systems in electrochemistry [4.277], polymer research [4.266, 4.278], catalysis [4.265, 4.271], selfassembling monolayers [4.267, 4.268], and protein adsorption [4.268, 4.279] have been investigated. [Pg.251]

Bale, M.D., Danielson, S.J., Daiss, J.L., Goppert, K.E., and Sutton, R.C. (1989) Influence of copolymer composition on protein adsorption and structural rearrangements at the polymer surface. J. Colloid Interface Sci. 132, 176-1874. [Pg.1045]

A change in the environment of a protein molecule, e.g. adsorption from aqueous solution onto a sorbent surface, may lead to a partial breakdown of its ordered structure, resulting in an increase of conformational entropy. This is a fundamental difference between protein adsorption and the adsorption of flexible polymers, for which attachment to a surface implies a loss of conformational entropy. [Pg.105]

Szleifer I (1997) Protein adsorption on surfaces with grafted polymers a theoretical approach. Biophys J 72 595-612 Tanford C (1973) The hydrophobic effect. John Wiley Sons, Inc., Hoboken Van Dulm P, Norde W, Lyklema J (1981) Ion participation in protein adsorption at solid surfaces. J Colloid Interf Sci 82 77-82 Zoungrana T, Findenegg GH, Norde W (1997) Structure, stability and activity of adsorbed ensymes. J Colloid Interf Sci 190 437-448 Zoungrana T, Norde W (1997) Thermal stability and enzymatic activity of a-chymotrypsin adsorbed on polystyrene surfaces. Colloid Surf B 9 157-167... [Pg.123]

For example, Asuri and his co-workers (Asuri et al., 2007) reported that the proteases attached to the surface of SWCNTs can create self-cleaning surfaces that resist protein adsorption. This kind of SWCNT-enzyme composite exhibited 30 times higher overall catalytic activity than control composites where the proteases were conjugated to a non-nanoscale graphite support. Importantly, the enzymes preserved more than 90% of their initial activity over 30% days in the liquid buffer, with only negligible amounts of enzymes leaching out. The result demonstrates that the nanocomposites of SWCNTs and polymers can act as hosts for enzymes and can prevent protein contamination on the surface of medical devices. We consider that SWCNTs may have the function as biocatalyst to improve the enzyme activity attached to the surface of CNTs. Our previous work also indirectly hints that CNTs could improve the bioactivity of enzymes such as Taq enzyme Cui et al. (2004). However, there are also adverse reports. CNTs can... [Pg.187]

T. Ives and W. M. Reichert, Protein adsorption on the surface of a thin-film polymer integrated optical waveguide, Appl. Spectrosc. 42, 68-72 (1988). [Pg.340]


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See also in sourсe #XX -- [ Pg.384 ]




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