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Patterned and switchable surfaces for biomaterial applications

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Chapter 1 - IntroductionFor some <strong>applications</strong> it has been desirable to adsorb DNA to negatively charged<strong>surfaces</strong>. This has been the case <strong>for</strong> atomic <strong>for</strong>ce microscopy (AFM) experimentswith DNA, which commonly require adsorption of DNA to atomically flat,hydrophilic mica <strong>and</strong> also <strong>for</strong> adsorption to silica, which is an important <strong>and</strong>ubiquitous material <strong>for</strong> many biodevices [20]. The electrostatic repulsion betweenDNA <strong>and</strong> mica or other negatively charged <strong>surfaces</strong> or particles can be overcome,enabling DNA adsorption, in the presence of a divalent cation such as Mg 2+ , whichcan act as bridging cations [20, 23, 43]. Generally, trivalent cations are moreeffective than divalent cations, which in turn are more effective than monovalentcations at enabling DNA adsorption. Hansma et al., [44] used AFM to study theeffect of the type of divalent cation on binding of dsDNA of lengths from 79-1057 bpto mica. High amounts of DNA adsorbed to mica in the presence of Ni, Co <strong>and</strong> Znions, however, weak adsorption was seen with Mn, Hg <strong>and</strong> Cd ions. This effect wasexplained in terms of the structure of mica <strong>and</strong> how each type of ion interacted withthe mica as opposed to a specific ion-DNA interaction, suggesting that the type ofion most suitable at enhancing DNA adsorption is dependant on the particularsubstratum surface.1.1.3. Surface manipulation of proteins <strong>and</strong> cellsMany biodevice <strong>applications</strong>, including tissue engineering, cell microarrays <strong>and</strong>implants [4, 45-47], require the ability to manipulate proteins, <strong>and</strong> concurrently cells,at interfaces. The fundamental nature of how proteins behave at <strong>surfaces</strong> dependslargely upon their primary structure, that is, the sequence of amino acids making upthe protein. There are four main properties of amino acids that influence thebehaviour of proteins; polar, non-polar, negatively charged <strong>and</strong> positively charged. It1-10

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