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Outer-Membrane Protease (OmpT) Based E. coli Sensing with Anionic Polythiophene and Unlabeled Peptide Substrate.
Sinsinbar, Gaurav; Gudlur, Sushanth; Wood, Sarah E; Ammanath, Gopal; Yildiz, Hakan U; Alagappan, Palaniappan; Mrksich, Milan; Liedberg, Bo.
Afiliación
  • Sinsinbar G; Centre for Biomimetic Sensor Science, School of Materials Science Engineering, Nanyang Technological University, 50 Nanyang Drive, Singapore, 637553, Singapore.
  • Gudlur S; Centre for Biomimetic Sensor Science, School of Materials Science Engineering, Nanyang Technological University, 50 Nanyang Drive, Singapore, 637553, Singapore.
  • Wood SE; Departments of Chemistry and Biomedical Engineering, Northwestern University, 2145 Sheridan Road, Evanston, IL, 60208, USA.
  • Ammanath G; Centre for Biomimetic Sensor Science, School of Materials Science Engineering, Nanyang Technological University, 50 Nanyang Drive, Singapore, 637553, Singapore.
  • Yildiz HU; Department of Chemistry, Izmir Institute of Technology, Urla, 35430, Izmir, Turkey.
  • Alagappan P; Centre for Biomimetic Sensor Science, School of Materials Science Engineering, Nanyang Technological University, 50 Nanyang Drive, Singapore, 637553, Singapore.
  • Mrksich M; Departments of Chemistry and Biomedical Engineering, Northwestern University, 2145 Sheridan Road, Evanston, IL, 60208, USA.
  • Liedberg B; Centre for Biomimetic Sensor Science, School of Materials Science Engineering, Nanyang Technological University, 50 Nanyang Drive, Singapore, 637553, Singapore.
Angew Chem Int Ed Engl ; 59(41): 18068-18077, 2020 10 05.
Article en En | MEDLINE | ID: mdl-32618102
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 (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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptido Hidrolasas / Péptidos / Polímeros / Tiofenos / Proteínas de la Membrana Bacteriana Externa / Proteínas de Escherichia coli Idioma: En Revista: Angew Chem Int Ed Engl Año: 2020 Tipo del documento: Article País de afiliación: Singapur Pais de publicación: Alemania
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptido Hidrolasas / Péptidos / Polímeros / Tiofenos / Proteínas de la Membrana Bacteriana Externa / Proteínas de Escherichia coli Idioma: En Revista: Angew Chem Int Ed Engl Año: 2020 Tipo del documento: Article País de afiliación: Singapur Pais de publicación: Alemania