Journal
BIOMACROMOLECULES
Volume 8, Issue 9, Pages 2781-2787Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bm7004774
Keywords
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Funding
- NHLBI NIH HHS [R01 HL084586, R01 HL084586-14A2] Funding Source: Medline
- NIBIB NIH HHS [R01 EB000278, R01 EB000278-13] Funding Source: Medline
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL084586] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING [R01EB000278] Funding Source: NIH RePORTER
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Pathogenesis in protein conformational diseases is initiated by changes in protein secondary structure. This molecular restructurina 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 beta-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 mu g 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.
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