Adsorption of proteins

Prime K L and Whitesides G M 1991 Self-assembled organio monolayers—model systems for studying adsorption of proteins at surfaoes Science 252 1164-7... 

Norde W 1986 Adsorption of proteins from solution at the solid-liquid interfaoe Adv. Colloid Interface Sc/. 25 267-340... 

Gilchrist, G.R., Direct fluidised bed adsorption of protein products from complex particulate feedstocks . PhD thesis, University of Birmingham, 1996. 

We used an anti-DNA antibody as an exploratory model system. The antibody was monoelonal from mouse sourees and its subelass was IgM. Mouse IgG (MW 1.5 x 10 Da) and IgM (MW 9 X 10 Da) antibodies from normal plasma, and bovine serum albumin were used for the eontrol measurements. To prevent the nonspeeilie adsorption of proteins to the uneovered, bare Au site in the modified eleetrode surfaee, the DNA-modified eleetrode prepared by the standard proeedure was further treated with aqueous 2-mercaptoethanol solution and was used for the measurements. 

Green, J. S. and Jorgenson, J. W., Minimizing adsorption of proteins on fused silica in capillary zone electrophoresis by the addition of alkali metal salts to the buffers, /. Chromatogr., 478, 63, 1989. 

Mechanical forces, such as shearing, shaking, and pressure, may also denature proteins [44,45], Shaking proteins may lead to inactivation owing to an increase in the area of the gas/liquid interface. At the interface, the protein unfolds and maximizes exposure of hydrophobic residues to the air. Surface denaturation may also occur at the protein/container interface and has been observed following adsorption of proteins to filter materials [46]. 

As seen in the comparison of mesoporous silica and PMO in protein adsorption behavior, the nature of the framework of mesoporous materials has unavoidable influence on the protein adsorption. Therefore, adsorption of protein on mesoporous structures composed of hydrophobic materials such as carbon is worthy of detailed investigation. In this section, systematic research on protein adsorption on mesoporous carbon materials by Vinu and coworkers is mainly introduced. 

Clay minerals or phyllosilicates are lamellar natural and synthetic materials with high surface area, cation exchange and swelling properties, exfoliation ability, variable surface charge density and hydrophobic/hydrophilic character [85], They are good host structures for intercalation or adsorption of organic molecules and macromolecules, particularly proteins. On the basis of the natural adsorption of proteins by clay minerals and various clay complexes that occurs in soils, many authors have investigated the use of clay and clay-derived materials as matrices for the immobilization of enzymes, either for environmental chemistry purpose or in the chemical and material industries. 

The adsorption of proteins onto surfaces is the oldest and easiest immobilization method. Adsorbing forces can be of different types Van der Waals interactions, ionic, hydrophobic or hydrogen bonding. The main advantages of this procedure are the simplicity of preparation and the little... 

To suppress cell adhesion on a material surface, one approach is to inhibit the adsorption of proteins. SAMs of alkanethiols that carry oligo(ethylene glycol) (OEG) [69] and phosphorylcholine [46, 70, 71] have been shown to prevent... 

Sigal GB, Mrksich M, Whitesides GM (1998) Effect of surface wettability on the adsorption of proteins and detergents. J Am Chem Soc 120 3464-3473... 

Ostuni E, Chapman RG, Holmlin RE, Takayama S, Whitesides GM (2001) A survey of structure-property relationships of surfaces that resist the adsorption of protein. Langmuir 17 5605... 

Prime KL, Whitesides GM (1993) Adsorption of proteins onto surfaces containing end-attached oligo(ethylene oxide) A model system using self-assembled monolayers. J Am Chem Soc 115 10714-10721... 

Prime, K.L., and Whitesides, G.M. (1991) Self-assembled organic monolayers model systems for studying adsorption of proteins at surfaces. Science 252, 1164. 

The physical adsorption of protein onto the surface of an electrode is a simple immobilization method. The adsorption is obtained by volatilizing the buffers containing proteins. The physical adsorption needs no chemical reagent, seldom activation and rinse, so that the bioactivities of the immobilized proteins can be retained well. However, the immobilized proteins are easy to break off from the electrode, which restrict broad applications of this method. Below are some examples of the physical adsorption of proteins immobilized on electrodes. 

Thickness of Adsorbed Protein Layers on Glass Adsorption of Proteins in Multilayers... 

To give an example both sensitivity coefficients are evaluated for the current sensor (see Sect. 10.3 for details). For the bulk detection of glucose this results in A bulk (rad) = 5.6 x 102 AC (g/ml), whereas for the adsorption of proteins on the sensor surface the overall sensitivity of the sensor is evaluated as A< >layer (rad) = 2.0 x 10 5 Am/A (fg/mm2). Measuring the phase change A< >,-, between any of the two channels i and j can thus give an estimation on the change in analyte concentrations between those two channels. If one channel (e.g., channel N) is used as a reference channel, then ACV = 0 and AmN = 0 and absolute analyte concentrations can be determined. 

TIRF has been used to study equilibrium adsorption of proteins to artificial surfaces both to learn about the surface properties of various biomaterials that have medical applications and also to test the TIRF technique itself. 

Electrochemistry of proteins is another case where electrode size affects the electrochemical results. Direct adsorption of proteins, such as enzymes, onto bulk metal surfaces frequently results in denaturation of the... 

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