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Bimodal fluorogenic sensing of matrix proteolytic signatures in lung cancer

Optical biosensing based on the activation of fluorescent reporters offers a powerful methodology for the real-time molecular interrogation of pathology. Here we report a first-in-class, bimodal fluorescent reporter strategy for the simultaneous and highly specific detection of two independent prote...

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Detalles Bibliográficos
Autores principales: Megia-Fernandez, Alicia, Mills, Bethany, Michels, Chesney, Chankeshwara, Sunay V., Krstajić, Nikola, Haslett, Chris, Dhaliwal, Kevin, Bradley, Mark
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6238727/
https://www.ncbi.nlm.nih.gov/pubmed/30175355
http://dx.doi.org/10.1039/c8ob01790e
Descripción
Sumario:Optical biosensing based on the activation of fluorescent reporters offers a powerful methodology for the real-time molecular interrogation of pathology. Here we report a first-in-class, bimodal fluorescent reporter strategy for the simultaneous and highly specific detection of two independent proteases (thrombin and matrix metalloproteases (MMPs)) pivotal in the fibroproliferative process surrounding lung cancer, based on a dual, multiplexing, peptide FRET system. This sophisticated synthetic smartprobe, with a molecular weight of 6 kDa, contains two independent fluorophores and quenchers that generate photonic signatures at two specific wavelengths upon activation by target enzymes within human lung cancer tissue.