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Biocompatibility proteins

Schaeferling M., Schiller S., Paul H., Kruschina M., Pavlickova P., Meerkamp M., Giammasi C., Kambhampati D., Application of self-assembly techniques in the design of biocompatible protein microarray surfaces, Electrophoresis 2002 23 3097-3105. [Pg.500]

C.J. Buchko, L.C. Chen, Y. Shen, D.C. Martin. 1999. Processing and mierostruetural characterization of porous biocompatible protein polymer thin films. [Pg.145]

Polymer surface modifications are omnipresent in applications where the surface properties of materials with favorable bulk properties are insufficient. By altering the surface characteristics using physical or chemical modification the desired surface properties may be achieved. Such treatments are required e.g. to enhance printability of films, the adhesion of paints, metal or other coatings, biocompatibility, protein resistances/reduced biofouling, etc. The diverse approaches met in practice include, among others, wet chemical and gas phase chemistry, plasma or corona, UV/ozone and flame treatments. In most cases surface chemical modification reactions take place that alter the surface energy in a desired way. For example,... [Pg.171]

Many natural materials are hydrophilic and show excellent biocompatibility. Proteins and carbohydrates of high molecular weight are extracted rather than synthesized chemically. On the down side, when the material is derived from mammalian tissue there is a certain risk of disease transmission and/or allergic reactions. Nevertheless, many biologically derived materials have just the desired properties for applications in nerve repair. [Pg.150]

Buchko C. J., Chen L. C., Shen Y., and Martin D. C., Processing and microstructural characterization of porous biocompatible protein potymer thin films. Polymer, 1999,40,1291-1 Wl. [Pg.256]

Buchko, C.J., K.M. Kozloff, and D.C. Martin. 2001. Surface characterization of porous, biocompatible protein polymer thin films. Biomaterials 22 1289. [Pg.164]

ELRs are a promising model of biocompatible protein-based polymers. The basic structure of ELRs involves a repeating sequence based on the recurring sequences found in the mammalian elastic protein elastin [4]. As far as their properties are concerned, some of their main characteristics are derived from those of the natural protein. Elastin is an extracellular matrix protein that is present in aU vertebrate connective tissue. Its functions include the provision of elasticity and resilience to tissues, such as large elastic blood vessels (aorta), elastic ligaments, lung and skin, which are subjected to repetitive and reversible deformation [5, 6]. [Pg.148]

Silva A, Silva-Freitas 6, Carvalho J, Pontes T, Araiijo-Neto R, Silva K, Carrl9o A, Egito E (2012) Advances in applied biotechnology (M Petre, Ed). InTech. doi 10.5772/1096 Badami AS, Kreke MR, Thompson MS, Riffle JS, Goldstein AS (2006) Effect of fiber diameter on spreading, proliferation, and differentiation of osteoblastic cells on electrospun poly(lactic acid) substrates. Biomaterials 27(4) 596-606. doi 10.1016/j.biomaterials.2005.05.084 Buchko CJ, Chen LC, Shen Y, Martin DC (1999) Processing and microstmctural characterization of porous biocompatible protein polymer thin films. Polymer 40(26) 7397-7407. doi 10.1016/ S0032-3861(98)00866-0... [Pg.424]

Briot, P. and M. Primet (1991). Catalytic oxidation of methane over palladimn supported on alumina. Effect of aging under reactants. Appfierf Catalysis 68(1) 301-314. Buchko, C. J., L. C. Chen, Y. Shen, and D. C. Martin (1999). Processing and micro-structural characterization of porous biocompatible protein polymer thin films. Polymer 40(26) 7397-7407. [Pg.332]


See other pages where Biocompatibility proteins is mentioned: [Pg.306]    [Pg.273]    [Pg.113]    [Pg.89]    [Pg.287]    [Pg.255]   


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