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|Title:||Outer-membrane protease (OmpT) based E. Coli sensing with anionic polythiophene and unlabeled peptide substrate||Authors:||Sinsinbar, Gaurav
Wood, Sarah E.
Yildiz, Hakan U.
|Keywords:||Engineering::Chemical engineering||Issue Date:||2020||Source:||Sinsinbar, G., Gudlur, S., Wood, S. E., Ammanath, G., Yildiz, H. U., Alagappan, P., Mrksich, M. & Liedberg, B. (2020). Outer-membrane protease (OmpT) based E. Coli sensing with anionic polythiophene and unlabeled peptide substrate. Angewandte Chemie, 132(41), 18224-18233. https://dx.doi.org/10.1002/ange.202008444||Project:||MOE2018-T2-1-025||Journal:||Angewandte Chemie||Abstract:||E. coli and Salmonella are two of the most common bacterial pathogens involved in foodborne and waterborne related deaths. Hence, it is critical to develop rapid and sensitive detection strategies for near-outbreak applications. Reported is a simple and specific assay to detect as low as 1 CFUmL@1 of E. coli in water within 6 hours by targeting the bacteriaQs surface protease activity. The assay relies on polythiophene acetic acid (PTAA) as an optical reporter and a short unlabeled peptide (LL37FRRV) previously optimized as a substrate for OmpT, an outer-membrane protease on E. coli. LL37FRRV interacts with PTAA to enhance its fluorescence while also inducing the formation of a helical PTAA-LL37FRRV construct, as confirmed by circular dichroism. However, in the presence of E. coli LL37FRRV is cleaved and can no longer affect the conformations and optical properties of PTAA. This ability to distinguish between an intact and cleaved peptide was investigated in detail using LL37FRRV sequence variants.||URI:||https://hdl.handle.net/10356/154573||ISSN:||0044-8249||DOI:||10.1002/ange.202008444||Rights:||© 2020 Wiley-VCH GmbH. All rights reserved.||Fulltext Permission:||none||Fulltext Availability:||No Fulltext|
|Appears in Collections:||MSE Journal Articles|
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