Polymers protein adsorption

Polymers, Protein Adsorption Andrade, J. D., Ed. Plenum Press ... 

In the studies on the blood-compatible polymers, protein adsorption is very important at least for two reasons. One reason is triggering of thrombus formation by protein adsorption as mentioned above. The other reason is that protein adsorption reflects the structure of the interface between the material and water, thus providing a good method for the analysis of the surface being in contact with water. 

Andrade, J.D. (Ed.), 1988. Surface and Interfacial Aspect of Biomedical Polymers. Protein Adsorption, vol. 2. Plenum, New York. 

JD Andrade. Surface and Interfacial Aspects of Biomedical Polymers Protein Adsorption. New York Plenum Press, 1985, Vol 2. 

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. 

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. 

Proteins may be covalently attached to the latex particle by a reaction of the chloromethyl group with a-amino groups of lysine residues. We studied this process (17) using bovine serum albumin as a model protein - the reaction is of considerable interest because latex-bound antigens or antibodies may be used for highly sensitive immunoassays. The temperature dependence of the rate of protein attachment to the latex particle was unusually small - this rate increased only by 27% when the temperature was raised from 25°C to 35°C. This suggests that non-covalent protein adsorption on the polymer is rate determining. On the other hand. the rate of chloride release increases in this temperature interval by a factor of 17 and while the protein is bound to the latex particle by only 2 bonds at 25°C, 22 bonds are formed at 35°C. 

J. D. Andrade and V. Hiady, Protein adsorption and materials biocompatibility A tutorial review and suggested hypotheses, Adv. Polymer Sci., 79, 1 (1986). 

Many kinds of nonbiodegradable vinyl-type hydrophilic polymers were also used in combination with aliphatic polyesters to prepare amphiphilic block copolymers. Two typical examples of the vinyl-polymers used are poly(/V-isopropylacrylamide) (PNIPAAm) [149-152] and poly(2-methacryloyloxyethyl phosphorylcholine) (PMPC) [153]. PNIPAAm is well known as a temperature-responsive polymer and has been used in biomedicine to provide smart materials. Temperature-responsive nanoparticles or polymer micelles could be prepared using PNIPAAm-6-PLA block copolymers [149-152]. PMPC is also a well-known biocompatible polymer that suppresses protein adsorption and platelet adhesion, and has been used as the hydrophilic outer shell of polymer micelles consisting of a block copolymer of PMPC -co-PLA [153]. Many other vinyl-type polymers used for PLA-based amphiphilic block copolymers were also introduced in a recent review [16]. 

Ishihara K, Nomura H, Mihara T et al (1998) Why do phospholipid polymers reduce protein adsorption J Biomed Mater Res 39 323-330... 

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. 

Discussing principles of protein adsorption may start from general trends observed for the adsorption of more simple flexible, highly solvated polymers, in particular, polyelectrolytes. 

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. 

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... 

Antrade, J. D., Principles of protein adsorption, In Surface and Interfacial Aspects of Biomed ical Polymers Antrade, J. D., Ed. Plenum Press, New York, 1985, Vol. 2... 

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... 

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). 

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