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|Title:||Post-polymerisation modification of surface chemical functionality and its effect on protein binding||Authors:||Choong, Cleo Swee Neo
Foord, J. S.
Parker, Emily M.
Moloney, Mark G.
|Issue Date:||2012||Source:||Choong, C. S. N., Foord, J. S., Griffiths, J.-P., Parker, E. M., Luo, B., Bora, M., et al. (2012). Post-polymerisation modification of surface chemical functionality and its effect on protein binding. New Journal of Chemistry, 36(5), 1187-1200.||Series/Report no.:||New journal of chemistry||Abstract:||Derivatisation of polystyrene by carbene insertions followed by diazonium coupling permits the introduction of diverse chemical functionality, providing access to materials with similar bulk properties, but in which surface chemical characteristics are systematically varied across a range of surface polarity, hydration and non-bonding interaction behaviour. Protein binding experiments with bovine serum albumin demonstrate that protein adhesion is dependent upon the identity of the surface chemical group, with tert-butyl, hexyl, dimethylamino, amino, and carboxyl modified systems all exhibiting higher levels of binding, while glycol, hydroxyl, and phosphonate give similar or lower levels of binding, relative to the control. This behaviour has been shown to be time dependent, and an approximate trend of protein binding with cheminformatic descriptors %PSA and contact angle was observed.||URI:||https://hdl.handle.net/10356/100978
|DOI:||http://dx.doi.org/10.1039/C2NJ00002D||Rights:||© 2012 The Royal Society of Chemistry and the Centre National de la Recherche Scientifique.||Fulltext Permission:||none||Fulltext Availability:||No Fulltext|
|Appears in Collections:||MSE Journal Articles|
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