Turner, Nicholas W.; Liu, Xiao; Piletsky, Sergey A.; Hlady, Vladimir and Britt, David W.
|DOI (Digital Object Identifier) Link:||http://dx.doi.org/10.1021/bm7004774|
|Google Scholar:||Look up in Google Scholar|
Pathogenesis in protein conformational diseases is initiated by changes in protein secondary structure. This molecular restructuring presents an opportunity for novel shape-based detection approaches, as protein molecular weight and chemistry are otherwise unaltered. Here we apply molecular imprinting to discriminate between distinct conformations of the model protein β-lactoglobulin (BLG). Thermal- and fluoro-alcohol-induced BLG isoforms were imprinted in thin films of 3-aminophenylboronic acid on quartz crystal microbalance chips. Enhanced rebinding of the template isoform was observed in all cases when compared to the binding of nontemplate isoforms over the concentration range of 1−100 μg mL-1. Furthermore, it was observed that the greater the changes in the secondary structure of the template protein the lower the binding of native BLG challenges to the imprint, suggesting a strong steric influence in the recognition system. This feasibility study is a first demonstration of molecular imprints for recognition of distinct conformations of the same protein.
|Item Type:||Journal Article|
|Copyright Holders:||2007 American Chemical Society|
|Academic Unit/Department:||Science > Life, Health and Chemical Sciences
|Interdisciplinary Research Centre:||Centre for Earth, Planetary, Space and Astronomical Research (CEPSAR)
Biomedical Research Network (BRN)
|Depositing User:||Nicholas Turner|
|Date Deposited:||02 Mar 2011 10:19|
|Last Modified:||18 Jan 2016 10:37|
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