Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/10451
Title: Outer-membrane protease (OmpT) based E.coli sensing with anionic polythiophene and unlabeled peptide substrate
Authors: Sinsinbar, Gaurav
Gudlur, Sushanth
Wood, Sarah E.
Ammanath, Gopal
Yıldız, Ümit Hakan
Alagappan, Palaniappan
Liedberg, Bo
Yıldız, Ümit Hakan
Keywords: enzymes
fluorescence
membrane proteins
pathogens
peptides
Issue Date: 2020
Publisher: John Wiley and Sons Inc.
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 CFU mL(-1)of E. coli in water within 6 hours by targeting the bacteria's surface protease activity. The assay relies on polythiophene acetic acid (PTAA) as an optical reporter and a short unlabeled peptide (LL37(FRRV)) previously optimized as a substrate for OmpT, an outer-membrane protease on E. coli. LL37(FRRV)interacts with PTAA to enhance its fluorescence while also inducing the formation of a helical PTAA-LL37(FRRV)construct, as confirmed by circular dichroism. However, in the presence of E. coli LL37(FRRV)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 LL37(FRRV)sequence variants.
Description: PubMed: 32618102
URI: https://doi.org/10.1002/anie.202008444
https://hdl.handle.net/10451
ISSN: 1433-7851
1521-3773
Appears in Collections:PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection

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