Please use this identifier to cite or link to this item: https://doi.org/10.1021/la200535c
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dc.titleImproving protein transfer efficiency and selectivity in affinity contact printing by using UV-modified surfaces
dc.contributor.authorChen, C.-H.
dc.contributor.authorYang, K.-L.
dc.date.accessioned2014-06-17T07:42:54Z
dc.date.available2014-06-17T07:42:54Z
dc.date.issued2011-05-03
dc.identifier.citationChen, C.-H., Yang, K.-L. (2011-05-03). Improving protein transfer efficiency and selectivity in affinity contact printing by using UV-modified surfaces. Langmuir 27 (9) : 5427-5432. ScholarBank@NUS Repository. https://doi.org/10.1021/la200535c
dc.identifier.issn07437463
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/64071
dc.description.abstractAffinity contact printing (αCP) is a technique that allows the selective capture of a target protein from solutions to a polymeric stamp decorated with an antibody, and then the target protein is printed onto a solid surface. The success of αCP critically relies on the precise control of protein-surface interactions. Here, we report a study on the effect of UV on the protein-surface interactions between protein and polydimethylsiloxane stamps and between protein and glass slides decorated with N,N-dimethyl-n-octadecyl-3- aminopropyltrimethoxysilyl chloride (DMOAP). Our results show that UV-modified surfaces can be used to improve the transfer efficiency and selectivity of proteins during αCP. For example, the protein transfer efficiency of human IgG onto a DMOAP-coated slide increases from 7.2% to 45.1% after the UV treatment. On the basis of these results, UV-modified surfaces were employed to develop a αCP system for protein detection. The detection limit of anti-IgG in this system is around 10 ng/mL, and the dynamic range is 4 orders of magnitude. © 2011 American Chemical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/la200535c
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentCHEMICAL & BIOMOLECULAR ENGINEERING
dc.description.doi10.1021/la200535c
dc.description.sourcetitleLangmuir
dc.description.volume27
dc.description.issue9
dc.description.page5427-5432
dc.description.codenLANGD
dc.identifier.isiut000289742500033
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