Post-polymerisation modification of surface chemical functionality and its effect on protein binding
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...
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sg-ntu-dr.10356-1009782020-06-01T10:21:18Z Post-polymerisation modification of surface chemical functionality and its effect on protein binding Choong, Cleo Swee Neo Griffiths, Jon-Paul Luo, Baiwen Bora, Meghali Foord, J. S. Parker, Emily M. Moloney, Mark G. School of Materials Science & Engineering 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. 2013-07-09T06:14:23Z 2019-12-06T20:31:41Z 2013-07-09T06:14:23Z 2019-12-06T20:31:41Z 2012 2012 Journal Article 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. https://hdl.handle.net/10356/100978 http://hdl.handle.net/10220/11063 10.1039/C2NJ00002D en New journal of chemistry © 2012 The Royal Society of Chemistry and the Centre National de la Recherche Scientifique. |
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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. |
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School of Materials Science & Engineering |
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School of Materials Science & Engineering Choong, Cleo Swee Neo Griffiths, Jon-Paul Luo, Baiwen Bora, Meghali Foord, J. S. Parker, Emily M. Moloney, Mark G. |
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Article |
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Choong, Cleo Swee Neo Griffiths, Jon-Paul Luo, Baiwen Bora, Meghali Foord, J. S. Parker, Emily M. Moloney, Mark G. |
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Choong, Cleo Swee Neo Griffiths, Jon-Paul Luo, Baiwen Bora, Meghali Foord, J. S. Parker, Emily M. Moloney, Mark G. Post-polymerisation modification of surface chemical functionality and its effect on protein binding |
author_sort |
Choong, Cleo Swee Neo |
title |
Post-polymerisation modification of surface chemical functionality and its effect on protein binding |
title_short |
Post-polymerisation modification of surface chemical functionality and its effect on protein binding |
title_full |
Post-polymerisation modification of surface chemical functionality and its effect on protein binding |
title_fullStr |
Post-polymerisation modification of surface chemical functionality and its effect on protein binding |
title_full_unstemmed |
Post-polymerisation modification of surface chemical functionality and its effect on protein binding |
title_sort |
post-polymerisation modification of surface chemical functionality and its effect on protein binding |
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2013 |
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https://hdl.handle.net/10356/100978 http://hdl.handle.net/10220/11063 |
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1681059719612989440 |