Please use this identifier to cite or link to this item: https://doi.org/10.1021/la200535c
Title: Improving protein transfer efficiency and selectivity in affinity contact printing by using UV-modified surfaces
Authors: Chen, C.-H. 
Yang, K.-L. 
Issue Date: 3-May-2011
Source: Chen, 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
Abstract: Affinity 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.
Source Title: Langmuir
URI: http://scholarbank.nus.edu.sg/handle/10635/64071
ISSN: 07437463
DOI: 10.1021/la200535c
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