Protein adsorption, surface

Steadman B L, Thompson K C, MIddaugh C R, Matsuno K, Vrona S, Lawson E Q and Lewis R V 1992 The effects of surface adsorption on the thermal stability of proteins Bioteoh. Bioengng. 40 8-15... 

Caputo A, Spamacci K, Ensoli B et al (2008) Functional polymeric nano/microparticles for surface adsorption and delivery of protein and DNA vaccines. Curr Drug Deliv 5 230-242... 

Tegoulia VA, Cooper SL (2000) Leukocyte adhesion on model surfaces under flow effects of surface chemistry, protein adsorption, and shear rate. J Biomed Mater Res 50 291-301... 

The surface of a solid may differ in many ways from its bulk composition. Especially, such solids as commercial carbon black may contain minor amounts of impurities (such as aromatics, phenol, carboxylic acid). This would render surface adsorption characteristics different from that of pure carbon. It is therefore essential that, in industrial production, quality control of the surface from different production batch is maintained. Otherwise, the surface properties will affect the application. Another example arises from the behavior of glass powder and its adsorption character for proteins. It has been found that if glass powder is left exposed to the... 

R. G. Lee, S.W. Kim, Adsorption of protein onto hydrophobic polymer surfaces adsorption isotherms and kinetics, J. Biomed. Mater. Res. 8 (1974) 251-259. 

Another attractive application of polymer brushes is directed toward a biointerface to tune the interaction of solid surfaces with biologically important materials such as proteins and biological cells. For example, it is important to prevent surface adsorption of proteins through nonspecific interactions, because the adsorbed protein often triggers a bio-fouling, e.g., the deposition of biological cells, bacteria and so on. In an effort to understand the process of protein adsorption, the interaction between proteins and brush surfaces has been modeled like the interaction with particles, the interaction with proteins is simplified into three generic modes. One is the primary adsorption. 

A two-dimensional micropatterned tissue can be easily obtained by utihz-ing the inherent differences in cell adhesiveness between different micropatterned photografted regions. This was attained by photoiniferter graft polymerization with a projection mask placed on an iniferter-derivatized surface. Since protein adsorption and cell adhesion are markedly suppressed on nonionic graft polymers, such as polyDMAm, any anchorage-dependent cells such as endothelial cell adhere and proliferate only on nonirradiated surfaces, resulting in the formation of a two-dimensional patterned tissue or cellular sheet (Fig. 24). 

The amount of surface adsorption of a number of proteins ranging in molecular mass from 6.5 to 670 kDa and isoelectric point (pi) from 4.3 to 10.5 to several commonly used container surfaces (glass vials either untreated, siliconized, sulfur treated or Purcoat treated plastic vials polyester + 0.3%, polyester 5x0, PP, and nylon). A 5-mL volume of protein solution was added to each vial, yielding a surface-to-volume ratio of 2.4cm2/mL. No correlation was found between the amount adsorbed and the molecular mass or isoelectric point, although glass surfaces appeared to bind more protein under the experimental conditions examined [156]. 

Polyethylene glycols are well known as protein-compatible molecules when coated or grafted onto surfaces. Both protein and platelet adsorptions to polyethylene glycol (PEG)-modified surfaces were shown to be reduced by PEG chains when attached to surfaces at one end of a molecule. Adsorption and platelet attachment were shown to be inversely proportional to the length of the PEG chain 100 monomer units provided minimal adsorption and adherence.- ... 

In TIRF protein adsorption experiments, it is desirable to correlate the intensity of excited fluorescence with excess protein concentration at the interface. Such an adsorbed layer is often in equilibrium with bulk-nonadsorbed protein molecules which are also situated inside the evanescent volume and thus contributing to the overall fluorescence. Various calibration schemes were proposed, using external nonadsorbing standards40,154 , internal standard in a form of protein solution together with a type of evanescent energy distribution calculation 154), and independent calibration of protein surface excess 155). Once the collected fluorescence intensity is correlated with the amount of adsorbed protein, TIRF can be applied in the study of various interactions between surface and protein. 

Quiquampoix, H., Abadie, J., Baron, M. H., Leprince, F., Matumoto-Pintro, P.T., Ratcliffe, R. G., and Staunton, S. (1995). Mechanisms and consequences of protein adsorption on soil mineral surfaces. In Proteins at Interfaces. Protein Adsorption on Soil Mineral Surfaces. Horbett, T. A., and Brash, J. L., eds., American Chemical Society Symposium Series 602, Washington, D.C., pp. 321-333. 

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